CN114836400A

CN114836400A - Enzyme participating in synthesis of bacteriophage diaminopurine and application thereof

Info

Publication number: CN114836400A
Application number: CN202210039767.XA
Authority: CN
Inventors: 张雁; 周彦; 仝杨
Original assignee: Tianjin University
Current assignee: Tianjin University
Priority date: 2021-01-14
Filing date: 2022-01-13
Publication date: 2022-08-02
Also published as: CN114836399A; CN114836399B; WO2022152192A1

Abstract

Enzymes involved in bacteriophage diaminopurine synthesis, including 2-aminodeoxyadenylate succinate (ADAS) synthetase, 2 '-deoxyadenine 5' -triphosphate triphosphatase (dATPase), dATP and dGTP pyrophosphate hydrolase, and uses of the enzymes are provided.

Description

Enzyme participating in synthesis of bacteriophage diaminopurine and application thereof

RELATED APPLICATIONS

The present application claims priority from chinese patent application No. 202110045505.X, filed on 14/1/2021, the entire contents of which are incorporated herein by reference in their entirety for all purposes.

Technical Field

This application relates generally to the fields of biochemistry and molecular biology and, in particular, discloses the Z base synthesis pathway of bacteriophage having a diaminopurine (also known as 2, 6-diaminopurine, 2-aminoadenine or Z base) containing genome, the enzymes involved and the use of these enzymes.

Background

Kirnos et al reported in 1977 that adenine (A) was completely replaced by Z in the genome of cyanobacterial phage (abbreviated herein as Cp) S-2L (1), but no pathway for such genome synthesis has been revealed so far. In view of important potential value and application of the Z base as a new base type, the research on the synthetic path of the Z base has scientific research and industrial application significance.

Summary of The Invention

In a first aspect, the present application provides a polypeptide having 2-aminodeoxyadenylate succinate (ADAS) synthetase activity, capable of catalyzing the formation of 2-aminodeoxyadenylate succinate with one or more of ATP, dATP, GTP, dGTP and dGMP and Asp as substrates, and having a catalytic motif for the polypeptide altered to GSxxKG compared to the GDxxKG catalytic motif for adenylate succinate synthetase (PurA), wherein x represents any amino acid residue.

Among the various 2-aminodeoxyadenylate succinate (ADAS) synthetase substrates identified herein, dGMP and Asp are common substrates and ATP, dATP, GTP, dGTP are variable substrates, where the 2-aminodeoxyadenylate succinate (ADAS) synthetase with ATP/dATP as substrate is referred to herein as PurZ (PurZ was first identified) and the 2-aminodeoxyadenylate succinate (ADAS) synthetase with GTP/dGTP as substrate is referred to herein as PurZ0(PurZ0 was isolated from a subsequent study in which PurZ was identified).

In some embodiments, when the polypeptide is aligned with the amino acid sequence of adenylate succinate synthetase from E.coli (SEQ ID NO:72), the amino acid sequence corresponding to SEQ ID NO: bit 303 of 72 is changed from R to L.

In some embodiments, when the polypeptide is identical to SEQ ID NO:2, has an amino acid sequence corresponding to SEQ ID NO: t at 274 bits of 2, N at 306 bits, F at 307 bits, and N at 309 bits.

In some embodiments, the polypeptide comprises SEQ ID NO:1-4, 9-69, 71 and 92-146, or SEQ ID NO:1-4, 9-69, 71 and 92-146, having one or more amino acid insertions, deletions and/or substitutions, or a variant of SEQ ID NO:1-4, 9-69, 71 and 92-146, or a fragment thereof retaining the catalytic motif.

In a second aspect, the present application provides a polypeptide having 2 ' -deoxyadenine 5 ' -triphosphate triphosphatolytic enzyme (dATPase) activity capable of catalyzing the hydrolysis of dATP to 2 ' -deoxyadenine (dA), comprising a metal and a ligand binding pocket.

In some embodiments, the polypeptide can also catalyze the hydrolysis of dADP and dAMP to 2' -deoxyadenine (dA).

In some embodiments, the polypeptide comprises Co ²⁺ As a divalent metal cofactor.

In some embodiments, the polypeptide comprises SEQ ID NO:5-7 and 73-91, or the sequence set forth in any one of SEQ ID NOs: 5-7 and 73-91 having one or more amino acid insertions, deletions and/or substitutions, or a variant of SEQ ID NO:5-7 and 73-91.

In a third aspect, the present application provides a polypeptide having dATP and dGTP pyrophosphate hydrolase activity capable of catalyzing the hydrolysis of dATP to dAMP and dGTP to dGMP, the polypeptide comprising a metal and a ligand binding pocket.

In some embodiments, the polypeptide comprises SEQ ID NO:8, or SEQ ID NO:8 having one or more amino acid insertions, deletions and/or substitutions, or a variant of SEQ ID NO:8, or a fragment of the sequence shown in figure 8, which retains the catalytic motif.

The polypeptides of the first to third aspects may be involved in the Z base synthesis pathway of a bacteriophage, wherein the polypeptide of the first aspect is the most critical one.

In a fourth aspect, the present application provides a nucleic acid molecule encoding a polypeptide according to the first to third aspects.

In a fifth aspect, the present application provides a vector comprising the nucleic acid molecule of the fourth aspect.

In a sixth aspect, the present application provides a method of engineering a bacteriophage comprising introducing into the genome of the bacteriophage a nucleic acid molecule encoding a polypeptide according to the first aspect, such that the bacteriophage expresses the polypeptide according to the first aspect.

In some embodiments, the method further comprises introducing into the genome of said bacteriophage a nucleic acid molecule encoding a polypeptide of the second aspect, to express said bacteriophage the polypeptide of the second aspect; and/or introducing a nucleic acid molecule encoding the polypeptide of the third aspect into the genome of the bacteriophage to express the polypeptide of the third aspect with the bacteriophage.

In some embodiments, the method further comprises introducing into the genome of said bacteriophage a nucleic acid molecule encoding an adenylosuccinate lyase (PurB), expressing the adenylosuccinate lyase (PurB) with said bacteriophage; and/or introducing into the genome of the bacteriophage a nucleic acid molecule encoding a GMP Kinase (GK) such that the bacteriophage expresses the GMP Kinase (GK).

In a seventh aspect, the present application provides a bacteriophage obtained by the method of the sixth aspect.

In an eighth aspect, the present application provides a host cell comprising a bacteriophage of the seventh aspect.

In some embodiments, the host cell is a bacterial cell.

In a ninth aspect, the application provides use of a bacteriophage of the seventh aspect or a host cell of the eighth aspect in diaminopurine deoxyribonucleotide (dZTP) synthesis, DNA origami, DNA-based data storage, antibacterial drug manufacture, bactericide manufacture or preservative manufacture.

Brief description of the drawings

FIG. 1 sequence and structural analysis of PurZ. A: the equivalent biosynthetic pathways for AMP and dZMP; b: a network of sequence similarity for putative PurZ; c: a homology model of SbPurZ; d: NMP binding sites in SbPurZ and EcPurA; e: sequence identification of NMP binding sites; f: purine interaction residues in the NTP binding site of PurZ/EcPurA; g: sequence identification of NTP binding sites; residue numbers are from EcPurA and Cp/SbPurZ.

FIG. 2 substrate specificity of SbPurZ, ApdATPase and ApDUF 550. A: substrate specificity of SbPurZ; b: complete reaction of SbPurZ, dGMP, ATP and Asp; c: asp, dGMP and ATP, omitting SbPurZ; d: a two-step reaction combining SbPurZ and EcPurB.

FIG. 3. putative biosynthetic pathway of the phage containing the Z genome. A: genome neighborhood of PurZ in phage; b: a biosynthetic pathway of the Z-containing genome; c: substrate specificity of ApdATPase; d: ApDUF 550.

FIG. 4 validation of Z base incorporation in the genome of Acinetobacter phage SH-Ab 15497. LC-UV detection (A) and extracted ion chromatogram (B) of dZ in phage DNA hydrolysate; the identity (D) of the host, phage, a and Z-containing ApPurZ PCR product with the corresponding NGS sequence Read Q score (C) and reading; cwDTW fraction distribution of host and phage readings (E); restriction enzyme digestion (F) of phage genomic DNA; SspI digests the A-containing ApPurZ PCR product, but does not digest the Z-containing ApPurZ PCR product (G).

FIG. 5 protein sequences of exemplary CpPurZ (PurA homolog) and CpdATPase for use in the present application. The difference between the two CpPurZ sequences is underlined.

FIG. 6A multiple sequence alignment of five different PurZ and EcPurA sequences. The dGMP, ATP and Asp binding residues are highlighted in a gray scale background, respectively. The positions of mutations in SbPurZ constructed in this application are indicated by boxes.

FIG. 7 shows the putative catalytic mechanism of SbPurZ. The atoms originating from dGMP, Asp and ATP are highlighted in different shades of grey respectively.

FIG. 8. sequence similarity network for PurA superfamily. Network with 10 ^-160 The E value of (a) shows, where each node represents a sequence having a sequence identity of 85% or more.

FIG. 9 SDS-PAGE gel analysis of recombinant proteins purified in the present application. FIGS. A-J show 4-20% SDS gels, lane 1 for molecular weight markers, and

lanes

2, 3 and 4 for 1, 2, 4. mu.g of purified protein. ApdATPase is a fusion protein containing an N-terminal MBP.

FIG. 10 PurZ enzyme Activity assay. A: time-dependent UV-Vis spectra of SbPurZ assay; B-D: UV-Vis spectra determined for ApPurZ, SpPurZ and VpPurZ; e: UV-Vis difference spectra in the SbPurZ assay, UV-Vis spectra at time 0 subtracted from each spectrum collected at different time points; f: SbPurZ-catalyzed time-dependent phosphate release was detected using phosphomolybdate assay. G: pH dependence of SbPurZ activity; h: determining the extinction coefficient (. epsilon.) of ADAS at 287 nm; i: ESI-MS detection of SbPurZ for 6-phosphoryl-dGMP formation in the absence of Asp (i.e., negative control); j: quantification of the phosphate released in the complete SbPurZ reaction mixture and in the reaction mixture omitting Asp; k: mass spectrometry of pure gmp, ATP and ADP; l: MS2 data for ADAS, dZMP, and dGMP in B and D of fig. 2.

Figure 11 enzyme kinetic analysis of PurZ. A: SbPurZ; b: SpPurZ; c: VpPurZ; d: ApPurZ; e: SbPurZ. In A-D, dGMP, ATP and Asp were used as substrates, and in E, dIMP, ATP, Asp were used as substrates.

FIG. 12 ESI-MS analysis of the Sp/ApPurZ-EcPurB-SeGK reaction. A: complete reaction of SpPurZ, dGMP, ATP, Asp, EcPurB and SeGK, indicating formation of the products dZDP and dZTP; b: complete reaction of ApPurZ, dGMP, ATP, Asp, EcPurB and SeGK, indicating formation of the products dZDP and dZTP.

FIG. 13 sequence and structural analysis of dATPase. A: metal and dATP binding motifs in dATPase homologs; b: homologous model of CpdATPase docked with dATP. Base and metal binding residues are labeled in gray scale, respectively.

FIG. 14 ESI-MS detection by dA formation of CpdATPase and ApdATPase. A: ESI (+) m/z spectra of CpdATPase reaction participated by dATP; b: the ESI (+) m/z spectrum of the CpdATPase reaction in which dADP is involved. C: ESI (+) m/z spectrum of reaction with dATP participating in ApdATPase; d: ESI (+) m/z spectra of the reaction involving dADP in ApdATPase.

FIG. 15 enzymatic activity and enzyme kinetics assay of dATPase. A: standard curves for phosphate, pyrophosphate and triphosphate. B: the metal dependence ratio of Cp/SpdATPase to chromophosphate is measured; c: substrate specificity of Cp/SpdATPase; D-F: kinetic constants of Cp/Sp/ApdATPase with dATP, dADP or dAMP as substrates.

FIG. 16 colorimetric phosphate assay for Cp/Sp/ApdATPase. A-C: Cp/Sp/ApdATPase reacted with dATP, dADP and dAMP, respectively.

FIG. 17 colorimetric and mass spectral characterization of ApDUF550 catalyzed reactions. A: 14-20% SDS gel results of purified ApDUF550, wherein lanes 1 are molecular weight markers and lanes 2-4 are 1, 2, 4 μ g of purified ApDUF 550; b: metal-dependent versus colored phosphate assay results for ApDUF 550; c and D: the ESI (-) m/z spectrum of the ApDUF550 catalytic reaction of participating in dATP and dGTP, form dAMP and dGMP respectively; the negative control omits ApDUF 550.

FIG. 18 ApPurZ PCR products with A and Z. A: UV-Vis spectra of ApPurZ PCR products containing A and Z; b: agarose gel analysis of ApPurZ PCR products containing A and Z.

FIG. 19 LC-MS/MS detection of dZ and Z in the genomic DNA of Acinetobacter phage SH-Ab 15497.

FIG. 20. change in nanopore signal with Z substitution. A: ApPurZ reads containing A match the expected signal; b: the corresponding Z-containing ApPurZ reads showed significant signal change compared to the expected signal; c: a to Z embellishments can be detected by Tombo (43) when using ApPurZ readings containing Z as input data and ApPurZ readings containing A as reference data. The KS test uses the maximum vertical difference between the two cumulative distribution curves. The D-statistic describes the difference between the two sets of data, with the larger D-statistic representing the greater probability of modifying the base.

FIG. 21. distribution of cwDTW alignment scores for ApPurZ with A and Z.

FIG. 22 restriction enzyme digestion of phage genomic DNA and PCR products containing Z. A: restriction maps of Sau3AI and TaqI on the genome of Acinetobacter phage SH-Ab 15497; b and C: restriction enzymes were used to digest phage genomic DNA and the Z-containing ApPurZ PCR product, respectively.

FIG. 23 substrate specificity of GpPurZ 0. A: substrate specificity of GpPurZ 0; b: detecting the absorption at the position of 220nm-340nm every 20 minutes by the GpPurZ0 full reaction; c: GpPurZ0 was measured separately using GTP/dGTP as the colorimetric phosphate for the substrate.

FIG. 24 shows the results of HPLC-MS detection of GpPurZ0 and EcPurB activities. A: reaction equation of GpPurZ0, PurB; b: asp, dGMP and GTP are reacted, and GpPurZ0 is omitted; c: GpPurZ0, dGMP and GTP react, and Asp is omitted; d: complete reaction of GpPurZ0, dGMP, GTP and Asp; e: a two-step reaction combining GpPurZ0 and EcPurB.

FIG. 25 shows crystal structure analysis of GpPurZ 0. A: the overall structure of GpPurZ 0; b: the active center interacting amino acids of GpPurZ0 and the electron cloud of the substrate GTP (hydrolyzed to GDP); c: global structural alignment of GpPurZ0 and VpPurZ (Vibrio phage phiVC 8); d: active center alignment of GpPurZ0 and VpPurZ crystal structures.

FIG. 26 construction of expression plasmids for the Z-genome of eukaryotic yeast. Left panel: the gene sequences of ApPurZ and dATPase are recombined and cloned to the gene map of plasmid pRS426 (pRS 426-ApPurZ-dATPase); right panel: the gene sequence of DUF550 was recombinantly cloned into the genetic map of plasmid pRS425 (pRS426-DUF 550).

FIG. 27 detection of dZ in the genome of yeast cells induced to express two plasmids, pRS426-ApPurZ-dATPase and pRS426-DUF 550. A, picture A: LC-UV detection of dZ in the yeast genome; b, extracting an ion chromatogram of the dZ.

Brief description of the sequences

SEQ ID NO:1 shows the amino acid sequence of the 2-aminodeoxyadenylate succinate (ADAS) synthetase (herein abbreviated as PurZ) of Acinetobacter phage (herein abbreviated as Ap) SH-Ab15497 identified and tested herein.

SEQ ID NO:2 shows the amino acid sequence of PurZ of the bacteriophage contig of the family sinobacillaceae (abbreviated herein as Sb) identified and tested by the present application.

SEQ ID NO: 3 shows the amino acid sequence of PurZ of the Salmonella phage (herein abbreviated Sp) identified and tested in the present application.

SEQ ID NO: 4 shows the amino acid sequence of PurZ of the Vibrio phage (Vibrio phase, abbreviated herein as Vp) identified and tested herein.

SEQ ID NO:5 shows the amino acid sequence of the 2 '-deoxyadenine 5' -triphosphate triphosphathydrolase (abbreviated herein as dATPase) of Acinetobacter bacteriophage (Ap) SH-Ab15497 identified and tested herein.

SEQ ID NO: 6 shows the amino acid sequence of the dATPase of the Salmonella phage (Sp) identified and tested herein.

SEQ ID NO:7 shows the amino acid sequence of the dATPase of the cyanobacterial phages (Cp) identified and tested in the present application.

SEQ ID NO: the amino acid sequences of dATP and dGTP pyrophosphate hydrolase (abbreviated herein as DUF550) of the Acinetobacter bacteriophage (Ap) SH-Ab15497 identified and tested herein are shown in FIG. 8.

SEQ ID NO: 9-69 show the amino acid sequences of PurZ or PurZ0 from different phages identified herein, the database entry information for which is as follows:

SEQ ID NO：9

＞tr|A0A2D0Z163|A0A2D0Z163_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage JSF15 OX＝1983598PE＝3SV＝1

SEQ ID NO：10

＞tr|A0A2D0YKL4|A0A2D0YKL4_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage JSF33 OX＝1983610 PE＝3 SV＝1

SEQ ID NO：11

＞tr|A0A2D0YMQ9|A0A2D0YMQ9_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage JSF9 OX＝1983616 PE＝3 SV＝1

SEQ ID NO：12

＞tr|A0A249XRS1|A0A249XRS1_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Temper16 OX＝2027887 GN＝TEMPER16_46PE＝3SV＝1

SEQ ID NO：13

＞tr|A0A222ZGD4|A0A222ZGD4_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Christian OX＝2015856GN＝46PE＝3SV＝1

SEQ ID NO：14

＞tr|A0A2S1GN16|A0A2S1GN16_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage Rostov 6 OX＝2116688 GN＝Rostov6_00061 PE＝3 SV＝1

SEQ ID NO：15

＞tr|A0A345KPY4|A0A345KPY4_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Sergei OX＝2250416 GN＝46 PE＝3 SV＝1

SEQ ID NO：16

＞tr|A0A345MLY7|A0A345MLY7_9CAUD Adenylosuccinate synthetase OS＝Siphoviridae sp.OX＝2170413 PE＝4 SV＝1

SEQ ID NO：17

＞tr|A0A2H4P933|A0A2H4P933_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Urla OX＝2047867 GN＝PHIRE_URLA_47 PE＝3 SV＝1

SEQ ID NO：18

＞tr|A0A2H4P9S1|A0A2H4P9S1_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage MeganNoll OX＝2047866 GN＝PHIRE_MEGANNOLL_49 PE＝3 SV＝1

SEQ ID NO：19

＞tr|A0A2H5BHJ6|A0A2H5BHJ6_9CAUD Adenylosuccinate synthetase OS＝Acinetobacter phage SH-Ab 15497 OX＝2060946 GN＝SHab15497_00039 PE＝3 SV＝1

SEQ ID NO：20

＞tr|A0A2L0V130|A0A2L0V130_9CAUD Adenylosuccinate synthetase OS＝Salmonella phage PMBT28 OX＝2081904 PE＝4 SV＝1

SEQ ID NO：21

＞tr|A0A3G8FRP9|A0A3G8FRP9_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Carpal OX＝2488956 GN＝48 PE＝3 SV＝1

SEQ ID NO：22

＞tr|A0A3G8FSG3|A0A3G8FSG3_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage CallieOMalley OX＝2488955 GN＝48 PE＝3 SV＝1

SEQ ID NO：23

＞tr|A0A3G8FU64|A0A3G8FU64_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Bodacious OX＝2488954 GN＝47 PE＝3 SV＝1

SEQ ID NO：24

＞tr|A0A386KAE0|A0A386KAE0_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Moki OX＝2315609 GN＝46 PE＝3 SV＝1

SEQ ID NO：25

＞tr|A0A3G3LZB6|A0A3G3LZB6_9CAUD PurA-like adenylosuccinate synthetase OS＝Microbacterium phage Goodman OX＝2484206 GN＝54 PE＝3 SV＝1

SEQ ID NO：26

＞tr|A0A3S9U8R5|A0A3S9U8R5_9CAUD PurA-like adenylosuccinate synthetase OS＝Streptomyces phage Hiyaa OX＝2499072 GN＝67 PE＝4 SV＝1

SEQ ID NO：27

＞tr|A0A3S9U9U2|A0A3S9U9U2_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage ChewChew OX＝2498999 GN＝47 PE＝3 SV＝1

SEQ ID NO：28

＞tr|A0A3S9UD05|A0A3S9UD05_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Huckleberry OX＝2499005 GN＝46 PE＝3 SV＝1

SEQ ID NO：29

＞tr|A0A3S9UEG9|A0A3S9UEG9_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Lennox OX＝2499007 GN＝46 PE＝3 SV＝1

SEQ ID NO：30

＞tr|A0A3G8FUL0|A0A3G8FUL0_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage BigMack OX＝2488953 GN＝47 PE＝3 SV＝1

SEQ ID NO：31

＞tr|A0A3G8FW66|A0A3G8FW66_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Beethoven OX＝2488952 GN＝48 PE＝3 SV＝1

SEO ID NO：32

＞tr|A0A3S9U891|A0A3S9U891_9CAUD Adenylosuccinate synthetase OS＝Alteromonas phage ZP6 OX＝2492447 PE＝4 SV＝1

SEQ ID NO：33

＞tr|A0A3S9UIP6|A0A3S9UIP6_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Savage2526 OX＝2499018 GN＝49 PE＝3 SV＝1

SEQ ID NO：34

＞tr|A0A3S9UJU3|A0A3S9UJU3_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage TattModd OX＝2499020 GN＝47 PE＝3 SV＝1

SEQ ID NO：35

＞tr|A0A3S9UQ44|A0A3S9UQ44_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage HeadNerd OX＝2499004 GN＝46 PE＝3 SV＝1

SEQ ID NO：36

＞tr|A0A3S9XAC5|A0A3S9XAC5_9CAUD Adenylosuccinate synthetase OS＝Bacillus phage vB_BpsS-140 OX＝2419621 GN＝purA PE＝3 SV＝1

SEQ ID NO：37

＞tr|A0A3S9UEN5|A0A3S9UEN5_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Litotes OX＝2499008 GN＝48 PE＝3 SV＝1

SEQ ID NO：38

＞tr|A0A3S9UG77|A0A3S9UG77_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage OurGirlNessie OX＝2499012 GN＝45 PE＝3 SV＝1

SEQ ID NO：39

＞tr|A0A3S9UGR8|A0A3S9UGR8_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Pterodactyl OX＝2499014 GN＝47 PE＝3 SV＝1

SEQ ID NO：40

＞tr|A0A3S9UHP3|A0A3S9UHP3_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Riverdale OX＝2499016 GN＝49 PE＝3 SV＝1

SEQ ID NO：41

＞tr|A0A4D6E427|A0A4D6E427_9CAUD Adenylosuccinate synthetase OS＝Microbacterium phage Theresita OX＝2562367 GN＝52 PE＝3 SV＝1

SEQ ID NO：42

＞tr|A0A4P8N3X9|A0A4P8N3X9_9CAUD PurA-like adenylosuccinate synthetase OS＝Microbacterium phage Sucha OX＝2565527 GN＝52 PE＝3 SV＝1

SEQ ID NO：43

＞tr|A0A514A4P2|A0A514A4P2_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage EstebanJulior OX＝2591067 GN＝47 PE＝3 SV＝1

SEQ ID NO：44

＞tr|A0A514A6Q5|A0A514A6Q5_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage DreamTeam OX＝2591066 GN＝46 PE＝3 SV＝1

SEQ ID NO：45

＞tr|A0A516KYX6A0A516KYX6_9VIRU Putative adenylosuccinate synthetase OS＝Prokaryotic dsDNA virus sp.OX＝2591644 GN＝Unbinned1529contig1001_3PE＝4SV＝1

SEQ ID NO：46

＞tr|A0A0A7HBP3|A0A0A7HBP3_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage J3 OX＝1558468GN＝J3_0027 PE＝3 SV＝1

SEQ ID NO：47

＞tr|A0A0A7HAZ3|A0A0A7HAZ3_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage CJY OX＝1558463 GN＝CJY_0027 PE＝3 SV＝1

SEQ ID NO：48

＞tr|A0A0A7HE19|A0A0A7HE19_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage H1 OX＝1558464 GN＝H1_0027 PE＝3 SV＝1

SEQ ID NO：49

＞tr|A0A0A7HA72|A0A0A7HA72_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage H2 SGB-2014 OX＝2268915 GN＝H2_0027PE＝3 SV＝1

SEQ ID NO：50

＞tr|A0A0A7HDV1|A0A0A7HDV1_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage H3 OX＝1558466 GN＝H3_0027 PE＝3 SV＝1

SEQ ID NO：51

＞tr|A0A1C9LZE7|A0A1C9LZE7_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage RcigaStruga OX＝1897763 GN＝SEA_RCIGASTRUGA_48 PE＝3 SV＝1

SEQ ID NO：52

＞tr|A0A1C9LZK6|A0A1C9LZK6_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Lucy OX＝1897761 GN＝SEA_LUCY_46 PE＝3 SV＝1

SEQ ID NO：53

＞tr|A0A1D8ESP0|A0A1D8ESP0_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Suppi OX＝1897553 GN＝SEA_SUPPI_49 PE＝3 SV＝1

SEQ ID NO：54

＞tr|A0A1D8ESU1|A0A1D8ESU1_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Vallejo OX＝1897554 GN＝SEA_VALLEJO_49 PE＝3 SV＝1

SEQ ID NO：55

＞tr|A0A0U4IL67|A0A0U4IL67_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Immaculata OX＝1772301 GN＝48 PE＝3 SV＝1

SEQ ID NO：56

＞tr|A0A0U4JDI1|A0A0U4JDI1_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage RAP15 OX＝1772312 GN＝50 PE＝3 SV＝1

SEQ ID NO：57

＞tr|A0A1I9SE08|A0A1I9SE08_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Oxynfrius OX＝1897429 GN＝SEA_OXYNFRIUS_49 PE＝3 SV＝1

SEQ ID NO：58

＞tr|A0A1I9SE71|A0A1I9SE71_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Greenhouse OX＝1897428 GN＝SEA_GREENHOUSE_50 PE＝3 SV＝1

SEQ ID NO：59

＞tr|A0A0U4B3X5|A0A0U4B3X5_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Joann OX＝1772303 GN＝50 PE＝3 SV＝1

SEQ ID NO：60

＞tr|A0A1V0S7A8|A0A1V0S7A8_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Korra OX＝1772304 GN＝49 PE＝3 SV＝1

SEQ ID NO：61

＞tr|A0A0U4JJ90|A0A0U4JJ90_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Pumancara OX＝1772311 GN＝46 PE＝3 SV＝1

SEQ ID NO：62

＞tr|A0A0U4IJU7|A0A0U4IJU7_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Wayne OX＝1772322 GN＝50 PE＝3 SV＝1

SEQ ID NO：63

＞tr|A0A0U4ITD6|A0A0U4ITD6_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Bennie OX＝1772293 GN＝47 PE＝3 SV＝1

SEQ ID NO：64

＞tr|A0A0U4IKR4|A0A0U4IKR4_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage DrRobert OX＝1772296 GN＝45 PE＝3 SV＝1

SEQ ID NO：65

＞tr|A0A0U4JKV6|A0A0U4JKV6_9CAUD PurA-like adenylosuccinate synthetase OS＝Arthrobacter phage Glenn OX＝1772297 GN＝50 PE＝3 SV＝1

SEQ ID NO：66

＞tr|G3FFN6|G3FFN6_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage phiVC8 OX＝1076759 GN＝phiVC8_p27 PE＝1 SV＝1

SEQ ID NO：67

＞tr|A0A0A7HAN6|A0A0A7HAN6_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage J2 OX＝1558467 GN＝J2_0027 PE＝3 SV＝1

SEQ ID NO：68

＞tr|A0A0A7H9T3|A0A0A7H9T3_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage QH OX＝1558469 GN＝QH_0026 PE＝3 SV＝1

SEQ ID NO：69

＞tr|Q6R6A8|Q6R6A8_9CAUD Adenylosuccinate synthetase OS＝Vibrio phage VP5 OX＝260827 GN＝purA PE＝3 SV＝1

SEQ ID NO: 70 shows the corresponding amino acid sequence of PurZ, GenBank _ AX955019.1, in the genome sequencing results reported in 2003 for cyanobacterial phage (Cp).

SEQ ID NO: 71 shows the amino acid sequence corresponding to PurZ in the genome sequencing results reported in 2018 of cyanobacterial phage (Cp), SRA _ SRR 8295598.

SEQ ID NO:72 shows the amino acid sequence of adenylate succinate synthetase (herein abbreviated as PurA) of E.coli (herein abbreviated as Ec) used in the analysis, comparison and testing herein.

SEQ ID NO: 73-91 show the amino acid sequences of dATPases from different phages identified herein, and their database entry information is as follows:

SEQ ID NO：73

＞tr|A0A3S9U872|A0A3S9U872_9CAUD Metal dependent phosphohydrolase OS＝Alteromonas phage ZP6 OX＝2492447 PE＝4 SV＝1

SEQ ID NO：74

＞tr|A0A3E0QWQ6|A0A3E0QWQ6_9BACT HD domain-containing protein OS＝Bacteroidetes bacterium OX＝1898104 GN＝DWQ49_09875 PE＝4 SV＝1

SEQ ID NO：75

＞tr|A0A3N5W4Z0|A0A3N5W4Z0_9CHLR HD domain-containing protein OS＝Chloroflexi bacterium OX＝2026724 GN＝EHM33_00540 PE＝4 SV＝1

SEQ ID NO：76

＞tr|A0A419GR34|A0A419GR34_9ACTN HD domain-containing protein OS＝Gaiellales bacterium OX＝2093372 GN＝C4534_06075 PE＝4 SV＝1

SEQ ID NO：77

＞tr|A0A0F9RMS3|A0A0F9RMS3_9ZZZZ Uncharacterized protein OS＝marine sediment metagenome OX＝412755 GN＝LCGC14_0626120 PE＝4 SV＝1

SEQ ID NO：78

＞tr|X6EBY6|X6EBY6_9RHIZ Phosphohydrolase OS＝Mesorhizobium sp.LNHC220B00 OX＝1287232 GN＝X739_11710 PE＝4 SV＝1

SEQ ID NO：79

＞tr|A0A1Z9IJG7|A0A1Z9IJG7_9BACT Uncharacterized protein OS＝Opitutales bacterium TMED158 OX＝1986794 GN＝CBD18_02345 PE＝4 SV＝1

SEQ ID NO：80

＞tr|A0A5C7KKG5|A0A5C7KKG5_9GAMM HD domain-containing protein OS＝Sinobacteraceae bacterium OX＝1969813 GN＝E6R08_06230 PE＝4 SV＝1

SEQ ID NO：81

＞tr|A0A0A7HDW4|A0A0A7HDW4_9CAUD HD domain-containing protein OS＝Vibrio phage CJY OX＝1558463 GN＝CJY_0025 PE＝4 SV＝1

SEO ID NO：82

＞tr|A0A0A7HA17|A0A0A7HA17_9CAUD Uncharacterized protein OS＝Vibrio phage H1 OX＝1558464 GN＝H1_0025 PE＝4 SV＝1

SEQ ID NO：83

＞tr|A0A0A7HDN4|A0A0A7HDN4_9CAUD HD domain-containing protein OS＝Vibrio phage H2 SGB-2014 OX＝2268915 GN＝H2_0025 PE＝4 SV＝1

SEQ ID NO：84

＞tr|A0A0A7HAK4|A0A0A7HAK4_9CAUD Uncharacterized protein OS＝Vibrio phage H3 OX＝1558466 GN＝H3_0025 PE＝4 SV＝1

SEQ ID NO：85

＞tr|A0A0A7HBK9|A0A0A7HBK9_9CAUD Uncharacterized protein OS＝Vibrio phage J2 OX＝1558467 GN＝J2_0025 PE＝4 SV＝1

SEQ ID NO：86

＞tr|A0A0A7HEL9|A0A0A7HEL9_9CAUD Uncharacterized protein OS＝Vibrio phage J3 OX＝1558468 GN＝J3_0025 PE＝4 SV＝1

SEQ ID NO：87

＞tr|A0A2D0Z4D9|A0A2D0Z4D9_9CAUD Hydrolase OS＝Vibrio phage JSF15 OX＝1983598 PE＝4 SV＝1

SEQ ID NO：88

＞tr|A0A2D0YMF2|A0A2D0YMF2_9CAUD Hydrolase OS＝Vibrio phage JSF33 OX＝1983610 PE＝4 SV＝1

SEQ ID NO：89

＞tr|A0A2D0Z988|A0A2D0Z988_9CAUD Hydrolase OS＝Vibrio phage JSF9 OX＝1983616 PE＝4 SV＝1

SEQ ID NO：90

＞tr|G3FFN4|G3FFN4_9CAUD Metal dependent phosphohydrolase OS＝Vibrio phage phiVC8 OX＝1076759 GN＝phiVC8_p25 PE＝4 SV＝1

SEQ ID NO：91

＞tr|Q6R6A9|Q6R6A9_9CAUD Uncharacterized protein OS＝Vibrio phage VP5 OX＝260827 PE＝4 SV＝1

the following table shows specific sequences of the 2-aminodeoxyadenylate succinate (ADAS) synthetases identified herein, distinguishing PurZ from PurZ 0.

Detailed Description

Unless otherwise indicated, terms used in the present application have meanings commonly understood by those skilled in the art.

Unless otherwise indicated, nucleic acids are written from left to right in the 5 'to 3' direction, respectively; amino acid sequences are written from left to right in the amino to carboxy direction. Numerical ranges include the numbers defining the range. Amino acids may be referred to herein by their commonly known three-letter symbols or by the one-letter symbols recommended by the IUPAC-IUB Biochemical nomenclature Commission. Similarly, nucleotides may be represented by commonly accepted single-letter codes. The terms defined above are more fully defined with reference to the specification as a whole.

When residue position numbering is described in this application for alignment of amino acid sequences, it refers to numbering other than the first methionine (M). For example, for an amino acid sequence with a first methionine (M), H10 refers to histidine (H) at position 10 after M.

The terms "polypeptide" and "protein" are used interchangeably herein to refer to polymers of amino acid residues and variants and synthetic and naturally occurring analogs thereof. Thus, these terms apply to naturally occurring amino acid polymers and naturally occurring chemical derivatives thereof, as well as amino acid polymers in which one or more amino acid residues are synthetic non-naturally occurring amino acids, such as chemical analogs of corresponding naturally occurring amino acids. Such derivatives include, for example, post-translational modifications and degradation products, including phosphorylated, glycosylated, oxidized, isomerized, carboxylated, and deaminated variants of polypeptide fragments.

The term "enzyme active center" as used herein refers to a site in an enzyme molecule that is capable of directly binding to a substrate molecule and catalyzing a chemical reaction on the substrate, which site becomes the active center of the enzyme.It is generally accepted that the active center is composed primarily of two functional sites: the first is a catalytic site where the substrate bond is broken or a new bond is formed to undergo a chemical change; the second is the binding site, by which the substrate of the enzyme binds to the enzyme molecule. The functional site is composed of a few amino acid residues which are relatively close to each other in the three-dimensional structure of the enzyme molecule or certain groups on the residues, which may be far apart in the primary structure and even located on different peptide chains, but are close to each other in the spatial conformation through the coiling and folding of the peptide chains; for enzymes requiring a coenzyme, the coenzyme molecule (e.g., metal ion Zn) ²⁺ And/or Mn ²⁺ ) Or a certain part of the structure of the coenzyme molecule is also a component of the functional site.

The term "amino acid" as used herein refers to a compound in which a hydrogen atom on a carbon atom of a carboxylic acid is replaced with an amino group, and the amino acid molecule contains both amino and carboxyl functional groups. Including naturally occurring and non-naturally occurring amino acids as well as amino acid analogs and mimetics. Naturally occurring amino acids include the 20 (L) -amino acids used in protein biosynthesis, as well as other amino acids, such as 4-hydroxyproline, hydroxylysine, carboxylated lysine, desmosine, isodesmosine, homocysteine, citrulline, and ornithine. Non-naturally occurring amino acids include, for example, (D) -amino acids, norleucine, norvaline, p-fluorophenylalanine, ethylmethionine, and the like, as known to those skilled in the art. Amino acid analogs include modified forms of naturally and non-naturally occurring amino acids. Such modifications may include, for example, substitution of chemical groups and moieties on the amino acids, or derivatization of the amino acids. Amino acid mimetics include, for example, organic structures that exhibit functionally similar properties, such as the charge and charge space characteristics of an amino acid. For example, the organic structure that mimics arginine (Arg or R) has a positively charged moiety that is located in a similar molecular space and has the same degree of mobility as the e-amino group of the side chain of the naturally occurring Arg amino acid. The mimetic also includes a constraining structure to maintain optimal steric and charge interactions of the amino acid or amino acid functional group. One skilled in the art can determine what structures constitute functionally equivalent amino acid analogs and amino acid mimetics.

The term "isoenzyme" as used herein refers to an enzyme that catalyzes the same reaction in vivo but differs in molecular structure.

The term "nucleic acid" as used herein refers to mRNA, RNA, cRNA, cDNA, or DNA, including single-stranded and double-stranded forms of DNA. The term generally refers to a polymeric form of nucleotides of at least 10 bases in length, which are ribonucleotides or deoxynucleotides or modified forms of either type of nucleotide.

The term "encoding" as used herein in the context of a particular nucleic acid means that the nucleic acid contains the necessary information to direct translation of the nucleotide sequence into a particular protein. The information encoding the protein is represented using a codon. A nucleic acid encoding a protein may comprise untranslated sequences (e.g., introns) located within translated regions of the nucleic acid or may lack such intervening untranslated sequences (e.g., as in cDNA).

As used herein, "full-length sequence" in reference to a particular polynucleotide or protein encoded thereby refers to the entire nucleic acid sequence or the entire amino acid sequence having a native (non-synthetic) endogenous sequence. The full-length polynucleotide encodes the full-length, catalytically active form of the particular protein.

The term "isolated" as used herein refers to a polypeptide or nucleic acid, or biologically active portion thereof, that is substantially or essentially free of components that normally accompany or react with the protein or nucleic acid as found in its naturally occurring environment. Thus, an isolated polypeptide or nucleic acid is substantially free of other cellular material or culture medium when produced by recombinant techniques, or substantially free of chemical precursors or other chemicals when chemically synthesized. With respect to DNA, an "isolated" is understood to mean a region that is present in a genome unless otherwise indicated or clearly judged from context.

The term "expression vector" as used herein is a nucleic acid construct, produced recombinantly or synthetically, with a series of specific nucleic acid elements that permit transcription of a particular nucleic acid in a host cell.

The term "host cell" as used herein refers to a cell that receives a foreign gene during transformation and transduction (infection). The host cell may be a eukaryotic cell such as a yeast cell or a prokaryotic cell such as E.coli. In the context of host cells involving bacteriophages, host cells refer primarily to bacteria.

Detailed description of the preferred embodiments

DNA modifications are formally and functionally distinct, but do not generally alter Watson-Crick base pairing. Diaminopurine (Z) is a unique exception because in cyanobacterial phages (cyanobacterial phages) it completely replaces adenine and forms three hydrogen bonds with thymine. However, the biosynthesis, species distribution and importance of the Z-containing genome have not been explored. In the present application, a multienzyme system supporting the synthesis of genes containing Z is reported. The inventors identified tens of phages with these enzymes worldwide, and further validated the Z-containing genome in the Acinetobacter (Acinetobacter) phage SH-Ab15497, a representative example of these phages, using LC-UV and mass spectrometry. One of the roles of the Z-containing genome is to confer a chemical advantage to the phage to circumvent the attack of host restriction enzymes. The discovery of biosynthetic pathways for Z-containing genomes has enabled the large-scale preparation of Z-DNA (i.e., conventional DNA in which A is replaced with Z) for a variety of applications.

2-amino deoxyadenylate succinate (ADAS) synthetase, referred to herein as PurZ or PurZ0, was the enzyme first identified and characterized by the inventors herein, and is a key enzyme involved in Z base synthesis. PurZ or PurZ0 is a broad homologue of PurA known in the art to be involved in adenine (A) synthesis, with similar reaction mechanisms (see A in FIG. 1), but differences in substrate specificity determine the differences in the reactions. The catalytic motif of PurA has been characterised and revealed, for GDxxKG, see for example positions 12-17 of EcPurA in figure 6, for all PurZ or PurZ0 identified herein, the catalytic motif has been changed to GSxxKG, and according to the inventors' analysis, the smaller volume of S replacing the larger volume of D can accommodate the additional 2-amino group of the substrate, resulting in different substrate selectivity and specificity. Therefore, GSxxKG is demonstrated to be a catalytic motif for PurZ or PurZ 0. In some embodiments, the catalytic motif of PurZ or PurZ0 is gsttgkg.

In some embodiments, when the polypeptide is aligned with the amino acid sequence of adenylate succinate synthetase from E.coli (SEQ ID NO:72, EcPurA), the amino acid sequence corresponding to SEQ ID NO: bit 303 of 72 is changed from R to L.

Sequence alignment is a technique commonly used by those skilled in the art and there are conventional alignment tools (e.g., BLASTn, BLASTp, BLASTx, etc.). Furthermore, since PurZ or PurZ0 is a family of homologues to which PurA belongs, alignment of the two is also easy to achieve. PurZ or PurZ0 is compared to PurA, for example, in EcPurA where position 303 is changed from R to the aliphatic amino acid L, which is consistent with PurZ or PurZ0 having a deoxyribonucleotide (rather than a ribonucleotide) substrate.

In some embodiments, when the polypeptide is identical to SEQ ID NO: 2(SbPurZ) has an amino acid sequence corresponding to SEQ ID NO: t at 274 bits of 2, N at 306 bits, F at 307 bits, and N at 309 bits. The above sites are relatively important residues identified by the inventors to have some effect on reactivity.

SEQ ID NO:1-4 are examples of PurZ identified and tested herein, SEQ ID NO: 71 is the PurZ amino acid sequence of cyanobacterial phage. SEQ ID NO: 9-69 and 92-146 are PurZ or PurZ0 sequences of other phages obtained by the inventors according to sequence similarity and evolutionary tree analysis in a database of known phage genes. By comparative analysis, they have catalytic motifs and important residues in line with the PurZ or PurZ0 examples identified and tested herein, which are expected to have PurZ or PurZ0 function.

The inventors have fully characterized the structure and function of PurZ or PurZ0, and identified catalytic motifs and important residues, on the basis of which insertions, deletions and/or substitutions of one or more amino acids of the non-catalytic and binding domains are not expected to affect PurZ or PurZ0 function. In some embodiments, the number of amino acid insertions, substitutions, and/or deletions is from 1 to 30, preferably from 1 to 20, more preferably from 1 to 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acid insertions, substitutions, and/or deletions.

Similarly, fragments obtained by appropriate truncation are expected to be functional given the knowledge of the catalytic motif and important residues.

In a second aspect, the present application provides a polypeptide having 2 ' -deoxyadenine 5 ' -triphosphate triphosphatase (dATPase) activity capable of catalyzing the hydrolysis of dATP to 2 ' -deoxyadenine (dA), comprising a metal and a ligand binding pocket. In some embodiments, the polypeptide can also catalyze the hydrolysis of dADP and dAMP to 2' -deoxyadenine (dA).

dATPase is another enzyme discovered and identified by the inventors to be involved in Z genome biosynthesis. Since the host to which the phage parasitizes may produce the precursor dATP that synthesizes the A base, one of the effects of dATPase involves promoting the synthesis of the Z-containing genome by specifically removing dATP and its precursor dADP, preventing A from being incorporated into the phage genome.

SEQ ID NO:5-7 are examples of dATPases identified and tested herein. Similarly, the inventors have also characterized the catalytic mechanism of dATPase, on the basis of which it would be expected to obtain variants and fragments with the same/similar dATPase function. SEQ ID NO: 73-91 are dATPase sequences of other phages obtained by the inventors according to sequence similarity and evolutionary tree analysis in a database of known phage genes. By comparative analysis, they have catalytic motifs and important residues consistent with the dATPase examples identified and tested herein, which are expected to have dATPase function.

DUF550 is another enzyme discovered and identified by the inventors to be involved in Z genome biosynthesis. DUF550 is able to catalyze the hydrolysis of dGTP to dGMP, which is one of the substrates of PurZ or PurZ0, and the presence of DUF550 increases the level of dZTP while also consuming dATP to further facilitate Z incorporation.

SEQ ID NO:8 is an example of a DUF550 identified and tested herein. Likewise, the inventors have characterized the catalytic mechanism of DUF550, on the basis of which it is expected that variants and fragments with the same/similar DUF550 function are obtained.

The polypeptides of the first to third aspects may be involved in the Z base synthesis pathway of a bacteriophage, wherein the polypeptide of the first aspect is the most critical one. dATPase and DUF550 are not involved in the synthesis reaction and contribute to the synthesis of the Z-containing genome.

Nucleic acid molecules that are coding sequences may be combined with other DNA sequences, such as promoters, polyadenylation signals, other restriction sites, multiple cloning sites, other coding segments, and the like.

Nucleic acids and fusions thereof can be prepared, manipulated, and/or expressed using any of a variety of mature techniques known and available in the art. For example, nucleic acid molecules encoding the polypeptides of the present application, or variants and fragments thereof, may be used in recombinant DNA molecules to direct expression of the polypeptides in appropriate host cells. Due to the inherent degeneracy of the genetic code, other DNA sequences encoding substantially identical or functionally equivalent amino acid sequences may also be used in the present application, and these sequences may be used to clone and express a given polypeptide.

In addition, nucleic acid molecules of the present application can be engineered using methods well known in the art, including but not limited to, changes in the cloning, processing, expression, and/or activity of the gene product.

In some embodiments, the nucleic acid molecule is produced by artificial synthesis, e.g., direct chemical synthesis or enzymatic synthesis.

In some embodiments, the nucleic acid molecule is produced by recombinant techniques.

In some embodiments, the nucleic acid molecule is an isolated nucleic acid molecule.

The nucleic acid molecule of the fourth aspect may be provided in a vector in the form of an expression cassette. The expression cassette may additionally comprise a 5' leader sequence which serves to enhance translation. In preparing the expression cassette, various DNA fragments may be manipulated to provide DNA sequences in the appropriate orientation and, where appropriate, in the appropriate reading frame. To this end, linkers or linkers may be employed to join the DNA fragments, or other manipulations may be involved to provide convenient restriction sites, remove excess DNA, remove restriction sites, and the like. For this purpose, in vitro mutagenesis, primer repair, restriction, annealing, re-substitution, such as transition and transversion, may be involved.

Phage engineering is a matter of skill in the art, and for engineered phages that naturally contain normal A base genomes, synthesis of the Z base is possible by introduction of PurZ or PurZ 0.

As described above, engineering further to introduce dATPase and DUF550 can promote synthesis of the Z-containing genome.

PurB and GK are required for genome synthesis, but may also be provided by the host bacteria.

In some embodiments, the host cell is a bacterial cell.

In a ninth aspect, the application provides use of a bacteriophage of the seventh aspect or a host cell of the eighth aspect in diaminopurine deoxyribonucleotide (dZTP) synthesis, DNA origami, DNA-based data storage, antibacterial drug manufacture, bactericide manufacture or preservative manufacture. In this application, the inventors report a Z genome-containing biosynthetic system that can facilitate the production of Z-substituted DNA, which may be subsequently used in a variety of emerging applications, such as DNA origami (23) and DNA-based data archiving, with great potential due to its high storage capacity (24). Introduction of Z-containing genome biosynthetic enzymes into engineered phages may expand their host range and efficacy, for example, have been successfully used clinically and for life-saving phage therapy, food preservation (27) and environmental purposes from multiple drug-resistant acinetobacter baumannii (25) or Mycobacterium abscessus (26) infection. Increasing base diversity has long been a complaint in the art (28-30), and work by the inventors suggests that nature has provided such a practice. Given that the Z base is found in merle, the inventors' work may help in interdisciplinary studies of biogenesis and celestial biology (31).

Examples

The following examples are illustrative only and are not intended to limit the scope of the embodiments of the present application or the scope of the appended claims.

Example 1 identification, characterization and testing of PurZ

Materials and methods

Annotation of the cyanobacterial phage S-2L genome and identification of CpPurZ

The whole genome of cyanobacterial phage S-2L has been sequenced and was subject to a related patent application (NCBI accession No.: AX955019, length: 45570bp, SEQ ID No.70) in 2003 (8) and re-sequenced using next generation sequencing technology (NGS) in 2018 (NCBI accession No.: SRR8295598, SEQ ID No. 71). NGS sequencing data was not assembled. Using SPAdes 3.14.0 (http:// cab. spbu. ru/software/spans /), the inventors assembled NGS reads onto 44485bp long scaffolds. NGS genomic sequences differ significantly from previously patented genomic sequences at many locations. To identify candidate genes involved in Z-containing genome biosynthesis, the inventors annotated two versions of the cyanobacterial phage S-2L genome using the FgenesV/FgenesV0 software from the SoftBerry platform (http:// www.softberry.com /). In the patent application genome, the PurZ gene is identified from 15407-14232 site, the gene length is 1176bp, and 391aa protein is coded. In the NGS genome, the PurZ gene was identified as beginning at position 15122 and ending at position 16202, with a gene length of 1080bp, encoding a 359aa protein. By alignment with other PurZ CDSs, the inventors found that the difference between the two versions is from C-terminal insertion deletions (indels) and that the NGS version should be the correct one.

PurZ-containing contigs in metagenome misidentified as bacterial origin may be of phage origin

Three contigs containing PurZ (GenBank: SSEA01000061.1, QQVW01000181.1, and NHHH01000025.1, the corresponding PurZ being the three orange nodes in a in fig. 2) were annotated as bacterial origin in NCBI, and were subjected to BLASTp search. The results show that almost all encoded proteins are highly similar to phage sequences, such as phage stop enzyme, capsid, tail fiber, tail loop and bottom plate proteins, suggesting that they are of phage rather than bacterial origin (table 2).

Homology modeling of CpPurZ, SbPurZ, CpdATPase and molecular docking

HHPred (32) was used to find templates for CpPurZ, SbPurZ and CpdATPase. Among the highest ranked structures, PDB 1CIB (EcPurA) (10) and 1MEZ (MmPurA) (33) were used as templates for modeling CpPurZ and SbPurZ, respectively, because these structures are complexed with all substrate/substrate mimetics or products. Both models of PurZ bind three substrates: dGMP, ATP and Asp.

For CpdATPase, PDB was selected: 5TK7(34) as template to establish a homology model for CpdATPase, PDB: 5TK7 is a Co ²⁺ Dependent oxoacin-A triphosphate/monophosphateA phosphatase or a dATP/dAMP phosphatase having only 18% overall sequence identity but having the same metal binding residues as CpdATPase.

All structural models were used with Prime v.5.3

The construct is described in Suite 2019-1. The model was then used for molecular docking and structural analysis. The inventor is in

Glide SP was used in Suite 2019-1 to dock KEGG compound (35) (metabolite pool contains about 18000 metabolites) to IMP and GTP binding pockets in PurZ. The highest ranked ligands from PurZ docking results indicate that IMP sites prefer nucleotides/deoxynucleotides with guanine bases, whereas GTP sites have no strong preference for bases. For CpdATPase, the inventors docked all nucleoside derivatives and dZTP from KEGG compounds to the substrate binding pocket. The ligand binding pocket of cpda tpase is rather open and can accommodate all the usual dntps.

In the course of this application, the crystal structure of VpPurZ complexed with one and two of the three substrate/substrate analogs is released in the protein database (PDB: 6FM1 series). The overall folding and active site structure were similar to the homology model of the inventors.

Sequence Similarity Networks (SSN) of the PurA superfamily and PurZ family

Using the web-based tool EFI-EST (https：//efi.igb.illinois.edu/efi-est/) (36) generating SSN of PurA superfamily (Pfam accession number: PF 00709). By Cytoscape 3.7.0(37) at 10 ^-160 The e value of (b) shows SSN, each node represents a set of sequences having > 85% sequence identity. The 76 proteins (62 from phage, 12 from metagenome, 2 from archaea) were putative PurZ. Their sequences were used to construct individual SSNs at 10 ^-70 The e value of (d) is shown. In the course of this application, 56 additional PurZ sequences were additionally found, shown in table 1.

Multiple sequence alignment of PurA and PurZ families

MAFFT version 7.450(38) was used to generate multiple sequence alignments of the PurA superfamily (Pfam: PF00709), the PurZ family, selected representative PurA/PurZ sequences, and CpdATPase homologs. Based on the multiple sequence alignment of PurA/PurZ and dATPase sequences, key residues for ligand binding were used to generate sequence identity by WebLogo 3 (39).

Genomic background of PurZ

Genomic Neighborhood Networks (GNNs) were generated using SSNs of the PurZ family using EFI-GNT (https:// EFI. igb. illinois. edu/EFI-GNT /) (40). 10 upstream and 10 downstream adjacent genes of PurZ were collected and analyzed. For noise filtering, the co-occurrence percentage is set to 5%.

Identification of restriction enzyme in Acinetobacter baumannii

By searching for "restriction endonucleases" in Acinetobacter baumannii, 26 potential restriction endonucleases were collected from UniProt. To identify authentic (bona fide) restriction endonucleases with a high degree of similarity to the characterized restriction endonucleases, Blastp was performed on the Swiss-Prot database. The results showed that 3 of the 26 restriction enzymes were identified: A0B2XQW9, A0A3R9RVJ0, and A0a241ZGY5, wherein A0B2XQW9 has 87.7% sequence identity to P00642(EcoRI) with a cleavage site of G/AATTC; A0A3R9RVJ0 has 75.9% sequence identity with P00640(PstI) with a cleavage site CTGCA/G; A0A241ZGY5 shares 59.9% sequence identity with P33562(BsuBI) with a CTGCA/G cleavage site. EcoRI and PstI were selected for further study.

Experimental materials

LB medium was purchased from Oxoid Limited (Hampshire, UK). Ultrapure deionized water from Millipore Direct-Q was used. TALON resins were purchased from Clontech Laboratories Inc (Califomia, USA). All protein purification chromatography experiments are described in

On a pure FPLC system (GE Healthcare, USA). dZTP was purchased from Trilink (California, USA). Other nucleotides were purchased from Sigma-Aldrich.

Gene synthesis and cloning

Codon-optimized gene fragments for purZ, dATase, EcPurB, SeGK, and ApDUF550 were synthesized by Genewiz Inc. (Suzhou, China) and inserted between NdeI and BamHI restriction sites in pET-28a (+) to express a plasmid with an N-terminal His ₆ A tagged protein. CpPurZ, ApdATPase and ApDUF550 were also inserted into the SspI restriction site of pET-28a (+) -HMT vector using the Gibson assembly cloning protocol. The resulting plasmid tandem contains: his 6-tag, Maltose Binding Protein (MBP) and TEV protease cleavage site, followed by the construct of interest, confirmed by sequencing. The EcPurB (UniProt: P0AB89) gene was amplified by PCR (forward primer CCAGAGCGGATCAGGAATGGAATTATCCTCACTGACCG; reverse primer CCAATTGAGATCTGCCATATGTTATTTCAGCTCATCAACCATCG) and inserted into pET-28a (+) vector using Gibson assembly to express His with an N-terminus ₆ A tagged protein.

Expression and purification of PurZ, PurB, dATPase, SeGK and ApDUF550

Coli BL21(DE3) cells were transformed with plasmids encoding the PurZ, PurB, dATPase, SeGK and ApDUF550 genes and plated on LB agar supplemented with 50. mu.g/mL kanamycin. Transformants were grown in LB medium (300mL) at 37 ℃ in a shaking incubator at 220 rpm. When OD is measured ₆₀₀ When about 0.8 was reached, the temperature was lowered to 18 ℃ and isopropyl beta-D-1-thiogalactopyranoside (IPTG) was added to a final concentration of 0.5mM to induce production of the protein of interest. After 16-20 hours, cells were harvested by centrifugation (6000 Xg, 10 minutes at 4 ℃).

The cells were resuspended in 15mL lysis buffer (50mM Tris-HCl, pH8.0, 1mM phenylmethanesulfonyl fluoride, 0.2mg/mL lysozyme, 0.03% Triton X-100 and 0.02mg/mL DNase I). The cell suspension was frozen in a-80 ℃ refrigerator, then thawed, and incubated in a 25 ℃ water bath for 30 minutes to allow cell lysis. 1.5mL of 11% streptomycin sulfate (dissolved in water) was added to the cell lysate, followed by gentle mixing and centrifugation (20000 Xg, 10 min at 4 ℃). The supernatant was filtered through a 0.22 μ M filter and loaded onto a 5mL talen cobalt column pre-equilibrated with buffer a (20mM HEPES (ph7.5), 5mM β -mercaptoethanol (BME), and 0.2M KCl). The column was washed with 10 Column Volumes (CV) of buffer a, and then the protein was eluted with 5CV buffer a containing 150mM imidazole. The eluate was dialyzed overnight against 2L of buffer B (20mM HEPES (pH7.5), 0.1M KCl and 1mM dithiothreitol) to remove imidazole, and then concentrated using a centrifugal concentrator (30K MWCO; Millipore). The concentration of the purified protein was calculated from the absorbance at 280nm using NanodROP ONE (Thermo SCIENTIFIC). Purified proteins with commercial protein markers (Genstar, Shenzhen) were detected on 4-20% SDS polyacrylamide gradient gels and visualized by Coomassie staining.

Ultraviolet-visible spectrophotometry and colorimetric analysis of PurZ

Will contain 20mM HEPES (pH7.5), 2mM dGMP, 1mM ATP, 2mM Mg ²⁺ 、5mM Asp-Na ⁺ And 5. mu.M Sb/Sp/Vp/ApPurZ of 50. mu.L of the reaction mixture were incubated at Room Temperature (RT) for 0-6 h. The absorbance was monitored at 220 to 340nm using a Nanodrop ONE (Thermo SCIENTIFIC). Quantitative phosphate (13) was determined using colorimetric phosphomolybdate assay.

Substrate-specific colorimetric phosphate assay for SbPurZ

The mixture will contain 20mM HEPES (pH7.5), 2mM dGMP (dImp, GMP or IMP), 1mM ATP (GTP), 2mM Mg ²⁺ 、5mM Asp-Na ⁺ (Asp-Na-free) ⁺ As blank) and 5 μ M SbPurZ were incubated for 1 hour at room temperature. Quantitative phosphate (13) was determined using colorimetric phosphomolybdate assay.

ESI-MS/MS analysis of SbPurZ-EcPurB reaction

Will contain 20mM Tris-HCl (pH8.0), 1mM dGMP, 0.5mM ATP, 2mM Mg ²⁺ 、5mM Asp-Na ⁺ And 5. mu.M SbPurZ of 300. mu.L reaction mixture incubated at room temperature for 1 hour. Alternative preparation omitting SbPurZ or Asp-Na ⁺ Two negative controls of (2). The reaction was then applied to a centrifuge concentrator (3K MWCO; Millipore). Using Q active ^TM HF/UltiMate ^TM ESI-MS/MS analysis of flow-through was performed on a 3000RSLCnano (thermo Fisher) instrument. The sample loading volume was 5. mu.L, and the loading rate was 0.2 mL/min. The SbPurZ assay was repeated in addition with 5. mu.M EcPurB.

Dependence of PurZ Activity on substrate concentration

Absorbance at 287nm of 200. mu.L of a reaction mixture containing 50mM HEPES (pH8.5), 2mM Mg in a 96-well plate was monitored at 15s intervals for 1-5 minutes at room temperature using a Tecan M200 plate reader ²⁺ 0.2-1. mu.M of PurZ enzyme (Sb/Sp/Vp/ApPurZ), three substrates at fixed concentrations (5mM Asp-Na) ⁺ 0.1mM ATP, dGMP) and changing the third substrate 500-0. mu.M Asp-Na ⁺ 125-0. mu.M ATP or 60-0. mu.M dGMP.

Dependence of SbPurZ Activity on dIMP, IMP and GMP concentration

Absorbance of 200. mu.L of a reaction mixture containing 50mM HEPES (pH8.5), 2mM Mg at 290nm (41) or 287nm in a 96-well plate was monitored at 30s intervals for 3-4 minutes at room temperature using a TecanM200 plate reader ²⁺ ，5mM Asp-Na ⁺ 0.1mM ATP, 100-0. mu.M dIMP, IMP or GMP and 5. mu.M SbPurZ wild-type or S15D mutant.

ESI-MS analysis of dATPase reaction

Containing 10mM Tris-HCl (pH7.5), 1mM dATP or 1mM dADP, 0.5mM Co ²⁺ And 0.1-2. mu.M Cp/ApdATPase 300. mu.L of the reaction mixture was incubated at room temperature for 1 hour. The negative control omits Cp/ApdATPase. The reaction mixture was then incubated in a boiling water bath for 3 minutes and the precipitated protein was removed by centrifugation (18000 Xg, 5 minutes). The supernatant was filtered and loaded onto an Agilent 6230TOF LC/MS instrument (Agilent Technologies, CA, USA) for ESI-MS analysis without liquid chromatography. The sample loading volume was 5. mu.L, and the loading rate was 0.2 mL/min.

ESI-MS analysis of ApDUF550 reactions

Containing 10mM Tris-HCl (pH7.5), 0.5mM dATP or dGTP, 2mM Co ²⁺ And 0.5. mu.M ApDUF550 for 0.5 hours at room temperature. The negative control omits ApDUF 550. The reaction mixture was then treated by removing the enzyme by a centrifuge concentrator (3K MWCO; Millipore) and loaded onto an Agilent 6230TOF LC/MS instrument (Agilent Technologies, CA., USA) for ESI-MS analysis on a liquid-free chromatography column. The sample loading volume was 5. mu.L, and the loading rate was 0.2 mL/min.

Substrate specificity of dATPase

Containing 10mM HEPES (pH7.5), 1mM (d) NTP and 2mM Mg ²⁺ 、2mM Co ²⁺ mu.L of the reaction mixture of 0.2. mu.M Cp/Sp/ApdATPase and 0.3. mu.M yeast inorganic pyrophosphatase 1(IPP1) was incubated at room temperature for 1 h. Quantitative triphosphate (13, 42) was determined using colorimetric phosphomolybdate assay.

Colorimetric pyrophosphate and phosphate assays for Cp/Sp/ApdATPase reactions

Will contain 10mM HEPES (pH7.5), 0.5mM dATP or dADP, 2mM Mg ²⁺ 、2mM Co ²⁺ 100 μ L of reaction mixture of 0.2 μ M Cp/Sp/ApdATPase and 0.3 μ M inorganic pyrophosphatase 1(IPP1) was incubated at room temperature for 1 h. Pyrophosphate (13) was quantified using a colorimetric phosphomolybdate assay. Will contain 10mM HEPES (pH7.5), 0.5mM dAMP, 2mM Co ²⁺ And 1 u M Cp/Sp/ApdATPase 100 u L reaction mixture at room temperature were incubated for 1 hours. Quantitative phosphate (13, 42) was determined using colorimetric phosphomolybdate assays.

dependence of dATPase activity on substrate concentration

Will contain 10mM HEPES (pH7.5), 600-0. mu.M dATP/dADP/dAMP, 2mM Mg ²⁺ 、2mM Co ²⁺ 0.04-0.8. mu.M Cp/Sp/ApdATPase and 0.3. mu.M IPP1 for 0-10 min at room temperature. The triphosphate, pyrophosphate and phosphate were quantified using colorimetric phosphomolybdate assays (13, 42).

Metal selectivity of dATPase

Will contain 10mM HEPES (pH7.5), 0.5mM dAMP, 2mM Co ²⁺ (or other divalent metal ion) and 1 u M Sp/CpdATPase 100 u L reaction mixture at room temperature for 1 hours. Quantitative phosphate (13, 42) was determined using colorimetric phosphomolybdate assays.

Site-directed mutagenesis of SbPurZ

Point mutations in the SbPurZ active site were introduced by site-directed mutagenesis and confirmed by sequencing. A25. mu.L PCR reaction contained 50ng of pET28a (+) -SbPurZ plasmid as template, 0.4. mu.M forward and reverse primers (Table 6) and Fast Alteration DNA polymerase (KM101 from TIANGEN, Beijing, China). The 17 cycles of PCR reaction mixture were digested with DpnI to remove template and then transformed into FDM competent cells (TIANGEN). SbPurZ muteins were expressed and purified as described for wild-type PurZ.

Substrate specificity of ApDUF550

Containing 10mM HEPES (pH7.5), 0.5mM (d) NTP, 2mM Mg ²⁺ 、2mM Co ²⁺ 100 μ L of the reaction mixture, 0.2 μ M ApDUF550 (blank without ApDUF550), and 0.3 μ M IPP1 were incubated at room temperature for 0.5 hours. Pyrophosphate formation was quantified using a colorimetric phosphomolybdate assay (13).

Metal selectivity of ApDUF550

Will contain 10mM HEPES (pH7.5), 0.5mM dATP, 2mM Co ²⁺ (or other metal ions), 0.3. mu.M IPP1(2mM Mg) ²⁺ ) And 0.2 u M HMT-ApDUF550 of the reaction mixture 100 u L at room temperature were incubated for 0.5 hours. Pyrophosphate (13) was quantified using a colorimetric phosphomolybdate assay.

PCR amplification of ApPurZ DNA fragments Using dATP or dZTP

The reaction system contained 20ng of pET28a (+) -ApPurZ, 0.2mM dNTP (dATP) or 0.2mM dNTP (dZTP (Trilink N-2003-1)), 0.5. mu.M forward primer (ATGAAGAAGGCGACCGTTATTT), 0.5. mu.M reverse primer (TCAAGCAATGTTTGATGATTTGTTAT), 1 XQ 5 reaction buffer and 1. mu. L Q5DNA polymerase (NEB M0491L). The reaction was performed by thermal cycling on a T100 thermal cycler (BIO-RAD) including initial denaturation at 98 ℃ for 30 seconds and 30 cycles (98 ℃ for 10 seconds, 60 ℃ for 15 seconds and 72 ℃ for 30 seconds). The PCR product was purified using StarPrep gel extraction kit (GenStar) according to the manufacturer's instructions. The concentration was then measured using a Nanodrop ONE (Thermo SCIENTIFIC) and the purity was assessed by agarose gel electrophoresis. 400ng of DNA was loaded onto each lane of the agarose gel. Restriction enzyme SspI (NEB R0132S) digested samples were also included in the gel analysis.

ESI-MS analysis of the Sp/ApPurZ-EcPurB-SeGK reaction

Will contain 20mM HEPES (pH8.5), 1mM dGMP, 1mM ATP, 5mM Mg ²⁺ 、5mM Asp-Na ⁺ mu.L of the reaction mixture of 5. mu.M Sp/ApPurZ and 5. mu.M EcPurB were incubated at room temperature for 4 hours or 0.5 hours. The enzyme was removed from the reaction mixture by means of a centrifuge concentrator (3K MWCO; Millipore), and the product contained in the flow-through served as a substrate for SeGK. Add 5. mu.M SeGK, 1mMATP and 5mM Mg ²⁺ And incubated at room temperature for an additional 45 minutes. The reaction mixture was again applied to a centrifuge concentrator (3 KMWCO; Millipore) and the protein retained. The flow-through was then loaded onto an Agilent 6230TOF LC/MS instrument (Agilent Technologies, CA, USA) for ESI-MS analysis without a liquid chromatography column. The sample loading volume was 5. mu.L, and the sample was loaded with water at a loading rate of 0.2 mL/min.

Acinetobacter phage SH-Ab15497 genome DNA extraction

Logarithmic growth phase (OD) ₆₀₀ 0.6-0.8) Acinetobacter baumannii strain 15497, acinetobacter bacteriophage SH-Ab15497 (10) ⁹ PFU/mL) in a volume ratio of 1: 4 into LB soft agar overlay (0.7% agar) at 37 ℃ for 7-8 hours. The lysate was then collected in SM buffer (50mM Tris-HCl (pH7.5), 100mM NaCl, 8mM MgSO 5) ₄ And 0.1g/L gelatin) were incubated overnight at 4 ℃ in a shaker at 100 rpm. Cell debris was removed by centrifugation at 10000 Xg for 10 minutes at 4 ℃ using a centrifuge. Genomic DNA of phage SH-Ab15497 was extracted using the lambda phage genomic DNA kit (Zoman Biotech, ZP 317-1).

HPLC-UV Spectroscopy and LC-MS/MS analysis of Acinetobacter phage SH-Ab15497 genomic DNA

Genomic DNA from Acinetobacter phage SH-Ab15497 was enzymatically digested under neutral conditions. Briefly, 5. mu.g of phage genomic DNA or positive control (4. mu.g of ApPurZ PCR product containing Z) or negative control (4. mu.g of ApPurZ PCR product containing A), 2. mu.L of DNase I (NEB0303AA), 0.008 units of phosphodiesterase I (Sigma P3243), 2. mu.L of alkaline phosphatase (Takara 2120a) and 15. mu.L of 10 Xreaction buffer (500mM Tris-HCl (pH7.5), 100mM NaCl, 10mM MgCl. RTM ₂ And 10mM ZnSO ₄ ) Was incubated overnight at 37 ℃ and applied to a centrifugal concentrator (3K MWCO; millipore) were centrifuged. The flow-through was analyzed using an Agilent 6420 Triple Quadrupole LC/MS instrument (Agilent Technologies, Calif., USA). LC separation was performed on a Syncronis aQ (150 mm. times.4.6 mm, 3 μm) column at a flow rate of 0.5mL/min at room temperature. 10mM NH prepared in water (solvent A) and methanol (solvent B) was used ₄ AC (pH4.6) as the mobile phase. The application time is 0-12 minAs a gradient, 20-32% solvent B. The sample loading volume was 10. mu.L with the UV detector set at 260 nm. Standard compounds included commercially available deoxynucleosides (dA, dT, dC and dG) and homemade dZ (a dZTP hydrolysate of alkaline phosphatase (Takara 2120a) incubated at 37 ℃ for 1 hour, followed by retention of the enzyme by centrifugation). 2 μ L of each standard compound (ca. 0.1 μ g) was loaded. Q active using a column equipped with the same LC ^TM HF/UltiMate ^TM ESI-MS/MS analysis of enzyme digested phage genomic DNA samples (10. mu.L) was performed using the same elution protocol using a 3000RSLCnano (thermo Fisher) instrument at a flow rate of 0.4 mL/min. Mass spectrometric detection was performed in the electrospray ionization (ESI) mode.

Restriction enzyme digestion of Acinetobacter phage SH-Ab15497 genomic DNA and Z-containing ApPurZ DNA

Restriction enzyme digestions were performed on 0.2-0.3. mu.g of phage genomic DNA or Z-containing ApPurZ PCR product in 20. mu.L of reaction mix according to the manufacturer's instructions.

Nanopore sequencing

SQK-LSK109(2019 edition) was used to construct natural DNA extracted from Acinetobacter phage SH-Ab15497 and a Z/A-containing ApPurZ PCR product library. The library was then loaded into a flow cell FLO-MIN106(R9.4, Oxford Nanopore Technologies) with over 1100 active single wells. The MiniON Mk1B sequencer was used for sequencing. Guppy 3.2.10 integrated in MinKNOW 3.6.5 was used for base calling.

Nanopore sequencing data quality analysis

From the initially collected phage DNA sample 200537 readings, the inventors looked at the BLASTn results (e-value cut-off: 10- ²⁰ ) Each reading was assigned to either a phage or a host. The results showed that 58611 reads mapped to phage SH-Ab15497 and 141926 reads mapped to its host. Reading identity is then calculated based on the BLASTn alignment. The summary document of Guppy 3.2.10 gave a reading Q score. Mass analysis of sequencing data for Z/A containing ApPurZ PCR products was calculated in the same manner as for phage samples.

Generating a mapping table of Z-containing hexamers

The original signal for each reading was extracted from the fast5 file by ont _ fast5_ api, and long (longer than 100) low variance regions were removed. The corresponding NGS form of the phage DNA sequence for each reading was extracted from the BLASTn results above. The original signal was then aligned to the phage genomic DNA sequence using cwDTW (21). Based on the alignment, cwDTW scores (absolute difference between normalized raw signal and normalized expected signal) were generated for each hexamer in the readings (21). Based on the cwDTW score for the hexamers, the median normalized signal for each hexamer in all reads was extracted to generate a customized mapping table. The custom mapping table is then used by the cwDTW to regenerate a new alignment file. By repeating the above process for 3 rounds, the cwDTW score distribution of phage reads was similar to host reads, indicating the validity of the final map.

Results, analysis and discussion

Kirnos et al reported in 1977 that A was completely replaced by Z in the genome of cyanobacterial phage S-2L (1). When Z is paired with a T base, three hydrogen bonds are formed (1, 2). The difference from other types of nucleobase modifications (3) is the unique role of Z in altering Watson-Crick base pairing, including altering the physical, chemical and mechanical properties of double-stranded DNA (2, 4-6). However, there have been no reports on biochemical characterization of enzymes required for synthesis of Z-containing genomes. Understanding the biosynthesis of the Z-containing genome will help to study the species distribution of the Z-containing genome. Although the Z base (7) is unambiguously identified in carbonaceous merle (and Z is therefore a significant source of organic compounds required for life to appear on early Earth), to date, the bacteriophage S-2L is the only organism known to have the Z base in its genome.

The inventors have found and reported for the first time that in the purine biosynthetic pathway, the S-2L genome contains an open reading frame encoding a homologue of adenylosuccinate synthetase (PurA) (8), which homologue is referred to herein as PurZ (FIG. 4). PurA and adenylosuccinate lyase (PurB) are known to catalyze the conversion of inosine 5 '-monophosphate (IMP) to adenosine 5' -monophosphate (AMP) in many organisms (panel a in fig. 1) (9). The present application proposes and demonstrates that PurZ participates in a similar reaction to provide Z nucleotides (panel a in figure 1).

To verify the inventors' hypothesis, the inventors first analyzed and identified PurZ of various phages using bioinformatics, followed by recombinant production and characterization (panel B in fig. 1 and table 1). A homology model was constructed for S-2LPurZ (CpPurZ) and its closest homolog, SbPurZ (FIG. 1, panel C and Table 1). Then, the active site of PurZ was compared with the active site of Escherichia coli PurA (EcPurA) (10). The substrates of PurA are IMP, guanosine 5' -triphosphate (GTP) and Asp, and PurA catalyzes the transfer of GTP γ -phosphate to IMP, followed by replacement of the phosphate with aspartate to form adenyl succinate (9). The catalytic residue Asp13(D) in the PurA GDxxKG motif is replaced in PurZ by a ser(s) residue (figures D and E in figure 1, and figure 6). Molecular modeling has shown that replacement of Asp by a smaller volume of Ser can accommodate additional 2-amino groups of the substrate (FIG. 1, panel D) and may also alter the catalytic mechanism (FIG. 7) as Asp abstracts protons from IMP in PurA (9-11). Multiple sequence alignment shows that, although Asp13 is highly conserved in PurA, the Asp → Ser substitution is a common feature among the several tens of putative PurZ sequences (fig. 1, panel E, as well as fig. 6, 8). Furthermore, the conserved R303(EcPurA numbering) used to form hydrogen bonds with the 2' -hydroxyl group of IMP ribose was replaced by aliphatic Leu278/279 in Cp/SbPurZ (FIG. 1, panel E and FIG. 6), consistent with the substrate being a deoxyribonucleotide (rather than a ribonucleotide).

The inventors screened a number of PurZ homologs, selected four of them (Ap/Sp/Vp/SbPurZ, SEQ ID NOs: 1-4) (FIG. 9, FIG. 10 and Table 1), and tested their enzymatic activities with 2 ' -deoxyguanosine 5 ' -monophosphate (dGMP), adenine 5 ' -triphosphate (ATP) and Asp as substrates (panel A in FIG. 1). The results are consistent with the inventors' homology model (fig. 1, panels D and F). Ap, Sp and VpPurZ were from phage isolates, and SbPurZ in the metagenomic contig should also be of phage origin (table 2).

Incubation of PurZ with saturating amounts of substrate showed a time-dependent change in the absorbance spectrum, indicating that a reaction occurred at the nucleobase. The UV-Vis difference spectrum obtained by subtracting the spectrum of the starting material from the spectrum of the product shows a maximum at 287nm (A-E in FIG. 10), which corresponds to dGMP (. lamda.) (λ _{Maximum of} ＝252nm)(12) To an analogous 2-amino-2 '-deoxyadenosine 5' -monophosphate (dZMP) (lambda) _{Maximum of} 247,280nm) substance (2). During the reaction, the absorbance (. DELTA.A) at 287nm, confirmed by colorimetric phosphomolybdate assay (F in FIGS. 2A and 10) (13) ₂₈₇ ) Is proportional to the release of phosphate.

No reaction was observed with guanosine 5 '-monophosphate (GMP) or IMP in place of dGMP or with other ribonucleoside 5' -triphosphates (NTP) in place of ATP, confirming the substrate specificity of the reaction. When dIMP was used with ATP and Asp, the enzyme retained 38% activity (panel A in FIG. 2). The optimum pH for the reaction was about 9.5 (FIG. 10, Panel G). Monitoring of Δ a using continuous spectrophotometry ₂₈₇ To study the Michaelis-Menten kinetics of PurZ (FIG. 10, panel H). For the four enzymes, k _cat In the range of 2.3-16.5min ^-1 K for dGMP and ATP _M 1.6-5.1 and 4.1-21.1. mu.M, respectively (FIG. 11 and Table 3). Apparent K of dGMP _M Much lower than the previously reported intracellular concentration of dGMP in bacteria (about 50. mu.M) (14). K of dIMP _cat /K _M Significantly (15 fold) lower k than the physiological substrate dGMP _cat /K _M 。

The reaction intermediates and products of PurZ were confirmed by electrospray ionization tandem mass spectrometry (ESI-MS/MS, B-D in FIG. 2 and I-L in FIG. 10). Co-incubation of SbPurZ with dGMP, ATP and Asp resulted in the appearance of two new peaks at m/z 426 and 461, corresponding to adenine 5' -diphosphate (ADP) and 2-aminodeoxyadenylate succinate (ADAS), respectively (B and C in fig. 2). Omission of Asp results in a new peak at m/z-426 that matches the mass of ADP and the putative reaction intermediate 6-phosphoryl-dGMP (I in figure 10). In the absence of Asp, no phosphate release was detected, which is consistent with its capture in 6-phosphoryl-dGMP (J in fig. 10). A similar intermediate, 6-phosphoryl-IMP (10), was observed in a complex of the structure of EcPurA crystallized in the presence of IMP, GTP and sodium aminoethyl hexanoate (hadacin).

Since cyanobacterial phage S-2L does not encode a homolog of PurB, the inventors hypothesized that subsequent transformation of ADAS into dZMP is catalyzed by PurB from the host (A and B in FIG. 3). Incubation of SbPurZ reaction products with recombinant EcPurB (E in fig. 9) resulted in disappearance of ADAS peak and appearance of a new peak at m/z 345, corresponding to dZMP (D in fig. 2), demonstrating that bacterial PurB is in fact capable of dZMP synthesis.

To investigate substrate selectivity, the inventors performed mutagenesis of substrate interacting residues in SbPurZ to the corresponding residues in EcPurA. All mutations impaired the activity of PurZ to varying degrees (table 4). Notably, the S15D mutation completely abolished SbPurZ activity, consistent with the role of S15 in the 2-amino group that houses dGMP (D in fig. 1). The T274G mutant showed K for Asp _M The 271-fold increase was consistent with the role of T274 in Asp binding (fig. 7). Three-residue mutants of N306T, F307K, and N309D that interact with adenine in ATP result in K for ATP _M An increase of 89-450 fold (Table 4), while none of them was reactive with GTP. Similarly, none of the mutants showed activity on IMP. The dZMP must be phosphorylated to form 2-amino-2 '-deoxyadenosine 5' -triphosphate (dZTP), which can then be incorporated into the phage genome by a polymerase. This reaction is effectively catalyzed by Salmonella enterica GMP kinase (SeGK), indicating that enzymes from the bacterial host can fulfill this function (B in fig. 3, J in fig. 9, and 12).

To investigate whether other enzymes are involved in Z-containing genome biosynthesis, the inventors examined the genomic environment of PurZ and identified a DNA polymerase, a hydrolase-like enzyme containing the HD domain, and a protein containing the DUF550 domain (A in FIG. 3).

The HD domain enzyme (also referred to herein as dATPase) appears in the genome of 20 phages containing PurZ (A in FIG. 3). These HD domain enzymes have highly conserved metal and ligand binding pockets, but their sequences are highly diverse (a in fig. 3 and fig. 13). The inventors prepared recombinant Cp/Ap/Sp HD enzymes (SEQ ID NOs: 5-7) (F-H in FIG. 9). Although they have only 24-34% sequence identity (A in FIG. 3), all three enzymes exhibit 2 ' -deoxyadenine 5 ' -triphosphate hydrolase (dATP enzyme) activity, catalyzing the hydrolysis of 2 ' -deoxyadenine 5 ' -triphosphate (dATP) to 2 ' -deoxyadenine (dA) and triphosphate, using Co ²⁺ The highest activity was obtained as a divalent metal cofactor (FIG. 3C, FIGS. 14-16, apparentk _cat ＝0.5-5.2s ^-1 Apparent K _M 6.5-74.8 μ M). Apparent K of dATP _M The intracellular concentration of dATP in the previously reported bacteria was within the range (15). The enzyme is highly specific for dATP and has much lower hydrolytic activity for NTP and other dNTPs (C in FIG. 3). The enzyme also catalyzes the hydrolysis of 2 '-deoxyadenine 5' -diphosphate (dADP) and 2 '-deoxyadenine 5' -monophosphate (dAMP) to dA, releasing pyrophosphate and phosphate, respectively (fig. 15, 16). Thus, a dATPase can promote Z-containing genome synthesis by specifically removing dATP and its precursor dADP from the host's pool of nucleotides (16), thereby preventing a from being incorporated into the phage genome.

Also of interest is a protein containing DUF550 domain, as it coexists with PurZ. Recombinant ApDUF550(SEQ ID NO: 8) exhibits dATP and 2 '-deoxyguanosine 5' -triphosphate (dGTP) pyrophosphohydrolase activities catalyzing the hydrolysis of dATP/dGTP to pyrophosphate and dAMP/dGMP, respectively, using Co ²⁺ The highest activity was obtained as a divalent metal cofactor with little or no activity on NTP and pyrimidine dntps (D in figure 3 and figure 17). Thus, this DUF 550-containing enzyme can act to provide dGMP as a substrate for PurZ, increasing the level of dZTP, while consuming dATP to further facilitate Z incorporation (B in fig. 3).

The identification of PurZ and other genes involved in dZTP biosynthesis and genome incorporation provides the basis for studying the appearance of Z-containing genomes in nature. The predicted PurZ sequences included 60 sequences from phage isolates and 13 sequences from phage contigs in the metagenome (B in fig. 1 and table 1). PurZ-containing phages mainly belong to the families of the Bacterionaceae (Podoviridae) and the Bacterionaceae (Siphoviridae) (B in FIG. 1). In the post-genomic era, chemical determination of nucleotide content or base composition is no longer a routine procedure, and the possibility of these phages containing modified purines in DNA may be overlooked. The inventors of the present application developed a protocol to confirm the genomic incorporation of Z and selected one of the phages, lysis Acinetobacter (Acinetobacter) phage SH-Ab15497, for further study (17). Phage DNA was prepared and digested with a combination of DNase I, phosphodiesterase I and alkaline phosphatase, followed by LC-UV spectrometry and LC-MS/MS analysis (A and B in FIG. 4). The digested products of phage DNA and Z-DNA (positive control, PCR product of ApPurZ using Q5 polymerase with dZTP instead of dATP in dNTP mix, fig. 18) had negligible amounts of dA (a in fig. 4) compared to normal DNA (also referred to herein as a-DNA, relative to Z-DNA). The UV peak was quantified using an extinction coefficient to give a molar ratio of deoxynucleosides according to Chargarraff's rule, with a ratio of dZ to dT of 0.99 and a ratio of dC to dG of 1.05. The mass of cation matching the dZ nucleoside and Z base was detected (B in FIG. 4 and FIG. 19). These results indicate that Z is almost completely (and possibly completely) replacing the pairing of A and T in the genome of SH-Ab15497, and that the Z-containing genome is not limited to cyanobacterial phage S-2L, and that the appearance of the Z-containing genome may be broader than previously understood.

Since the phage DNA extracts will contain more or less varying amounts of host DNA fragments, the inventors performed nanopore sequencing of crude extracts to show that the quality of phage reads (quantified by Q-score, read identity and cwDTW alignment score) is similar to that of the Z-DNA control, while the quality of host reads is similar to that of normal DNA (C-E in FIG. 4 and FIGS. 20, 21) (18-20). Nanopore signals were assigned to approximately 100M reads of each of phage and host DNA, which allowed the inventors to statistically analyze the data and conclude that: phage DNA is almost adenine-free, while Z is unlikely to be incorporated into host DNA.

The function of various phage DNA modifications is to avoid attack by the host's restriction enzymes (3). Genomic DNA from S-2L has been reported to be resistant to most restriction enzymes (21, 22). To confirm this general applicability to Z-containing genomes, the inventors investigated the susceptibility of SH-Ab15497 genomic DNA and Z-PCR products to restriction enzyme digestion. The inventors have observed that: the DNA containing the Z substitution from both sources was resistant to digestion by enzymes containing one or more A in all recognition sites, including two close homologs of host endogenous DNA restriction enzymes (EcoRI and PstI). The only exception is TaqI, which is known to be able to tolerate a variety of DNA modifications (21). In contrast, both HaeIII and Sau96I recognized GC-only sequences, allowing easy digestion of phage DNA and Z-DNA controls (F and G in FIG. 4, FIG. 22, Table 5). Thus, one evolutionary advantage conferred by a Z-containing genome may be the ability to escape restriction enzyme digestion in a variety of bacteria. The inventors noted that no significant degradation was observed for phage DNA digested with Sau3AI, whereas for Sau3AI phage DNA contained more than 200 recognition sites, which is apparently consistent with the complete replacement of a with Z in the phage genome (fig. 22). The inventors further confirmed that PurZ-containing phages were widely distributed on earth (data not shown).

Table 1 putative PurZ screened and characterized in this application (italicized bold indicates the tested species).

"N/A": not applicable to

Table 3 kinetic parameters of PurZ.

Example 2 identification, characterization and testing of PurZ0

Based on the 2-aminodeoxyadenylate succinate (ADAS) synthetase identified in example 1, the inventors obtained more members of the 2-aminodeoxyadenylate succinate (ADAS) synthetase family of phages, including the amino acid sequence of SEQ ID NO: 9-69 and 92-146. By comparative analysis, they have the same catalytic motifs and important residues as the PurZ examples identified and tested in example 1, and are expected to function identically. Furthermore, by further structural analysis, the inventors found that part of the ADAS synthetase family members use GTP/dGTP and dGMP and Asp as reaction substrates, which is different from the example PurZ of example 1 which uses ATP/dATP and dGMP and Asp as reaction substrates, but the overall reaction route is very close. For the purpose of distinction, 2-aminodeoxyadenylate succinate (ADAS) synthetase with ATP/dATP as substrate is referred to as PurZ, and 2-aminodeoxyadenylate succinate (ADAS) synthetase with GTP/dGTP as substrate is referred to as PurZ 0.

This example characterizes and tests PurZ0 with GpPurZ0 (species: Gordonia phase Archimedes, Uniprot ID: A0A7L7SI10, SEQ ID NO: 121)).

The substrate specificity test and the assay method for combined action with PurB were similar to those of example 1 (except that the enzyme and the variable substrate were replaced, and the conditions were similar), and the results are shown in FIGS. 23 and 24, which confirmed the substrate specificity of GpPurZ0 using GTP/dGTP as a substrate and the detection results of GpPurZ0 in combination with high performance liquid chromatography-mass spectrometry of EcPurB activity.

The method for analyzing the GpPurZ0 crystal structure is as follows:

for the crystallization of GpPurZ0 protein, the protein obtained from TALON column was purified in 2L buffer [20mM Tris-HCl, pH7.5, 5mM BME]Dialyzed for 3 hours, and then applied to a 10mL Q Sepharose anion exchange column. Elution was performed with a linear gradient of buffer containing 300 to 700mM KCl. The protein containing a significant peak of GpPurZ0 was collected and concentrated to a final volume of 5mL using a centrifugal concentrator (30K MWCO; Millipore). However, the device is not suitable for use in a kitchenThen, the protein solution was injected into a buffer [20mM Tris-HCl, pH7.5, 0.2M KCl, 1mM dithiothreitol ]]Pre-equilibrated Superdex200 molecular sieve column (300mL) and eluted with buffer B. The gel filtration column was re-concentrated and washed with storage buffer [10mM HEPES/KOH, pH 7.4, 50mM KCl, 1mM Tris- (2-carboxyethyl) -phosphine hydrochloride]Buffer exchange was performed. The final concentration of the protein was adjusted to 10 mg/mL. The preliminary screening of GpPurZ0 crystals was performed by sitting-drop method in a 96-well plate using a crystallization robot system (Gryphon, Art Robbins). The optimum conditions for producing crystals were 1.26M ammonium sulfate and 0.2M lithium sulfate, 0.1M Tris pH8.5 and 5mM GTP. Crystallization reagents plus 25% glycerol were used as cryoprotectants and the crystals were rapidly cooled in liquid nitrogen. The resolution is collected at SSRF 18U (Shanghai synchrotron radiation light source)

The diffraction data of (1). Data were processed using HKL3000 software. Molecular substitutions were performed on the pheix software using the crystal structure model created by the website PHYRE 2. The structure was constructed manually using Coot software from the electron cloud trends and further optimized in pheenix software, and then uploaded to the RCSB protein database (accession code 7VF 6). The appendix table contains data on the crystal structure collected and finally optimized (table 7). All structure maps were generated using UCSF Chimera (fig. 25).

Table 7 data collection and optimized data statistics for crystals of GpPurZ 0.

According to sequence analysis, PurZ and PurZ0 are identical in the dGMP active site and are both GSxxKG (where x represents any amino acid residue, typically located at positions 13-18 of the amino acid sequence); but differs between the ATP/dATP and GTP/dGTP active sites in that the ATP/dATP active site of PurZ is nxxnxn/Q (where x represents any amino acid residue, usually located before or after position 300 of the amino acid sequence) and the GTP/dGTP active site of PurZ0 is T/SxxD (where x represents any amino acid residue, usually also located before or after position 300 of the amino acid sequence), from which PurZ and PurZ0 can be distinguished.

Example 3 Yeast application test

The gene sequences of ApPurZ and dATPase (see example 1) were cloned recombinantly into plasmid pRS426 (uracil-deficient), and the gene sequences of DUF550 (see example 1) were cloned recombinantly into plasmid pRS425 (leucine-deficient) by homologous recombination (FIG. 26). After gene sequencing was correct, both plasmids were transformed into yeast and plated on uracil and leucine deficient yeast synthetic solid media. After the successful transformation of the plasmid with the target gene is confirmed by PCR, a single colony is selected from the plasmid, cultured at 30 ℃ until the OD600 reaches 0.8, and added with a galactose inducer to induce the overexpression of ApPurZ, dATPase and DUF550 proteins. After 18h (OD ═ 3.5), cells were collected by high-speed centrifugation, and the yeast genome was extracted. And carrying out high performance liquid chromatography and mass spectrometry combined detection on the extracted yeast genome. The yeast genome induced by galactose over-expression of the three proteins had dZ production. By integration of the dZ uv chromatogram and quantitative calculation of the combined extinction coefficient, 20% dA was replaced by dZ on the yeast genome (fig. 27). As shown in the results of fig. 27, in the genomic DNA of galactose-induced yeast cells, (dZ + dA): dT is about 0.85, dZ: (dZ + dA) was about 0.2.

Although exemplary embodiments of the inventions of the present application have been described above, those skilled in the art will be able to make modifications and improvements to the exemplary embodiments described herein without departing from the spirit and scope of the present application, and variations and equivalents resulting therefrom also fall within the scope of the present application.

Reference to the literature

1.M.D.Kirnos，I.Y..Khudyakov，N.I.Alexandrushkina，B.F.Vanyushin，2-aminoadenine is an adenine substitutingfor a base in S-2L cyanophage DNA.Nature 270，369-370(1977).

2.I.Y..Khudyakov，M.D.Kirnos，N.I.Alexandrushkina，B.F.Vanyushin，Cyanophage S-2L contains DNA with 2，6-diaminopurine substituted for adenine.Virology 88，8-18(1978).

3.P.Weigele，E.A.Raleigh，Biosynthesis and function of modified bases in bacteria and their viruses.Chem.Rev.116，12655-12687(2016).

4.C.Cheong，I.Tinoco，Jr.，A.Chollet，Thermodynamic studies ofbase pairing involving 2，6-diaminopurine.Nucleic Acids Res.16，5115-5122(1988).

5.J.Sagi，E.Szakonyi，M.Vorlickova，J.Kypr，Unusual contribution of 2-aminoadenine to the thermostability of DNA.J.Biomol.Struct.Dyn.13，1035-1041(1996).

6.M.Cristofalo et al.，Nanomechanics of Diaminopurine-Substituted DNA.Biophys.J.116，760-771(2019).

7.M.P.Callahan et al.，Carbonaceous meteorites contain a wide range of extraterrestrial nucleobases.Proc.Natl.Acad.Sci.U.S.A.108，13995-13998(2011).

8.P.Marliere，Patent WO2003093461.(2003).

9.R.B.Honzatko，H.J.Fromm，Structure-function studies of adenylosuccinate synthetase from Escherichia coli.Arch.Biochem.Biophys.370，1-8(1999).

10.Z.Hou，M.Cashel，H.J.Fromm，R.B.Honzatko.Effectors of the stringent response target the active site of Escherichia coli adenylosuccinate synthetase.J.Biol.Chem.274，17505-17510(1999).

11.C.Kang，N.Sun，R.B.Honzatko，H.J.Fromm，Replacement of Asp333with Asn bv site-directed mutagenesis changes the substrate specificity of Escherichia coli adenylosuccinate synthetase fromguanosine 5′-triphosphate to xanthosine 5′-triphosphate.J.Biol.Chem.269，24046-24049(1994).

12.M.J.Cavaluzzi，P.N.Borer，Revised UV extinction coefficients for nucleoside-5′-monophosphates and unpaired DNA and RNA.Nucleic Acids Res.32，e13(2004).

13.G.Hua et al.，Characterization of santalene synthases using an inorganic pyrophosphatase coupled colorimetric assay.Anal.Biochem.547，26-36(2018).

14.B.D.Bennett et al.，Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli.Nat.Chem.Biol.5，593-599(2009).

15.B.R.Bochner，B.N.Ames，Complete analvsis of cellular nucleotides by two-dimensional thin layer chromatography.J.Biol.Chem.257，9759-9769(1982).

16.B.L.Greene et al.，Ribonucleotide Reductases：Structure，Chemistry，and Metabolism Suggest New Therapeutic Targets.Annu.Rev.Biochem.89，45-75(2020).

17.Y.Hua et al.，Characterization and whole genome analysis of a novel bacteriophage SH-Ab 15497 against multidrug resistant Acinetobacater baummanii.Acta Biochim.Biophys.Sin.(Shanghai) 51，1079-1081(2019).

18.J.J.Kasianowicz.E.Brandin，D.Branton，D.W.Deamer， characterization of individual polynucleotide molecules using a membrane channel..Proc.Natl..Acad.Sci.U.S.A.93，13770-13773(1996).

19.L.Xu，M.Seki，Recent advances in the detection of base modifications using the Nanopore sequencer..J.Hum.Genet.65，25-33(2020).

20.R.Han，Y.Li，X.Gao，S.Wang，An accurate and rapid continuous wavelet dynamic time warping algorithm for end-to-end mapping in ultra-long nanopore sequencing.Bioinformatics 34，i722-i731(2018).

21.M.Szekeres，A.V.Matveyev，Cleavage and sequence recognition of 2，6-diaminopurine-containing DNA by site-specific endonucleases.FEBS Lett.222，89-94(1987).

22.A.Chollet，E.Kawashima，DNA containing the base analogue 2-aminoadenine：preparation，use as hybridization probes and cleavage by restriction endonucleases.Nucleic Acids Res.16，305-317(1988).

23.P.W.Rothemund，Folding DNA to create nanoscale shapes and patterns.Nature 440，297-302(2006).

24.L.Ceze，J.Nivala，K.Strauss，Molecular digital data storage using DNA.Nat.Rev.Genet.20，456-466(2019).

25.R.T.Schooley et al.，Development and use of personalized bacteriophage-based therapeutic cocktails to treat a patient with a disseminated resistant Acinetobacter baumannii infection.Antimicrob.Agents Chemother.61，e00954-17(2017).

26.R.M.Dedrick et al.，Engineered bacteriophages for treatment of a patient with a disseminated drug-resistant Mycobacterium abscessus.Nat.Med.25，730-733(2019)

27.Z.D.Moye，J.Woolston，A.Sulakvelidze，Bacteriophage Applications for Food Production and Processing.Viruses 10，205(2018).

28.Y.Zhang et al.，A semi-synthetic organism that stores and retrieves increased genetic information.Nature 551，644-647(2017).

29.S.Hoshika et al.，Hachimoji DNA and RNA：A genetic system with eight building blocks.Science 363，884-887(2019).

30.D.A.Malyshev et al.，A semi-synthetic organism with an expanded genetic alphabet.Nature 509，385-388(2014).

31.J.Gollihar，M.Levy，A.D.Ellington，Many paths to the origin of life.Science 343，259-260(2014).

32.L.Zimmermann et al.，A completely reimplemented MPI bioinformatics toolkit with a new HHpred server at its core.J.Mol.Biol.430，2237-2243(2018).

33.C.V.Iancu，T.Borza，H.J.Fromm，R.B.HonZatko，Feedback inhibition and product complexes of recombinant mouse muscle adenylosuccinate synthetase.J.Biol.Chem.277，40536-40543(2002).

34.J.Bridwell-Rabb，G.Kang，A.Zhong，H.W.Liu，C.L.Drennan，An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis.Proc.Natl.Acad.Sci.U.S.A.113，13750-13755(2016).

35.M.Kanehisa，S.Goto，S.Kawashima，A.Nakaya，The KEGG databases at GenomeNet.Nucleic Acids Res.30，42-46(2002).

36.J.A.Gerlt et al.，Enzyme function initiative-enzyme similarity tool(EFI-EST)：A web tool for generating protein sequence similarity networks.Biochim.Biophys.Acta.1854，1019-1037(2015).

37.P.Shannon et al.，Cytoscape：a software environment for integrated models of biomolecular interaction networks.Genome Res.13，2498-2504(2003).

38.K.Katoh，D.M.Standley，MAFFT multiple sequence alignment software vetsion 7：improvements in performance and usability.Mol.Biol.Evol.30，772-780(2013).

39.G.E.Crooks，G.Hon，J.M.Chandonia，S.E.Brenner，WebLogo：a sequence logo generator.Genome Res.14，1188-1190(2004).

40.J.A.Gerlt，Genomic Enzymology：Web tools for leveraging protein family sequence-function space and genome context to discover hovel functions.Biochemistry 56，4293-4308(2017).

41.S.Mehrotra，H.Balaram，Kinetic characterization of adenylosuccinate synthetase from the thermophilic archaea Methanocaldococcus jannaschii.Biochemistry 46，12821-12832(2007).

42.G..Kohn et al.，High inorganic triphosphatase activities in bacteria and mammalian cells：identification of the enzymes involved.PLoS One 7，e43879(2012).

43.M.Stoiber et al.，De novo identification of DNA modifications enabled by genome-guided nanopore signal processing.bioRxiv，094672v2(2017).

Sequence listing

<110> Tianjin university

<120> enzyme involved in synthesis of bacteriophage diaminopurine and use thereof

<130> 21C13552CN

<150> 202110045505.X

<151> 2021-01-14

<160> 146

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<210> 1

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<213> Acinetobacter phage SH-Ab15497 (Acinetobacter phase SH-Ab 15497)

<400> 1

Met Lys Lys Ala Thr Val Ile Cys Asp Met Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Phe Leu Ala Glu Arg Asp Gln Pro Asp Val

20 25 30

Val Val Thr Ala Trp Ser Ala Asn Ala Gly His Thr Tyr Ile Asn Arg

35 40 45

Glu Gly Arg Lys Trp Val His Cys Met Leu Ala Asn Gly Ile Val Ser

50 55 60

Pro Lys Leu Lys Ala Val Leu Ile Gly Gly Gly Ser Gln Met Ser Ile

65 70 75 80

Pro Thr Leu Ile Ser Glu Ile Met Gly Ser Leu Asp Ile Leu Gln Gly

85 90 95

Lys Ser Ile Leu Ile His Glu Asn Ala Cys Ile Ile Gln Gln Arg His

100 105 110

Val Glu Glu Glu Ala Gly Pro Met Thr Lys Ile Gly Ser Thr Lys Lys

115 120 125

Gly Cys Gly Ala Ala Met Met Glu Lys Ile Arg Arg Asn Pro Glu Ser

130 135 140

Lys Ile Val Ala Lys Asp Phe Ile Asp Asp Gly Leu Glu Ile Pro Asp

145 150 155 160

Phe Lys Leu Asp Gly Thr Val Gly Phe Lys Asp Ile Ser Arg His Phe

165 170 175

Glu Glu Leu Gly Val Cys Ile Lys Val Val Ser Asn Glu Val Tyr Leu

180 185 190

Ala Val Leu His Lys Ala Glu Arg Val Gln Val Glu Gly Ala Gln Gly

195 200 205

Phe Ser Leu Gly Leu His Asn Gly Phe Tyr Pro Tyr Val Thr Ser Arg

210 215 220

Glu Cys Thr Pro Ala Gln Ile Cys Ser Asp Cys Asn Val Pro Ile Ser

225 230 235 240

Met Val Asp Lys Val Val Gly Thr Met Arg Thr Tyr Pro Ile Arg Val

245 250 255

Ala Asn Arg Phe Asp Asp Glu Gly Lys Met Val Gly Trp Ser Gly Pro

260 265 270

Cys Tyr Ser Asp Gln Thr Glu Leu Thr Trp Glu Gln Met Gly Val Thr

275 280 285

Pro Glu Lys Thr Thr Val Thr Lys Leu Thr Arg Arg Ile Phe Ser Phe

290 295 300

Ser Arg Met Gln Thr Arg Gln Ala Met Leu Val Cys Met Pro Asp Glu

305 310 315 320

Ile Phe Leu Asn Phe Ala Asn Tyr Cys Ala Ser Glu Asp Glu Leu Ala

325 330 335

Ser Ile Ile Glu Val Ile Ser Asn Glu Gly Gly Asp Val Ser Tyr Ile

340 345 350

Gly Trp Gly Asp Ser Ala Ala His Ile Glu Thr Thr Leu Glu Gly Asp

355 360 365

Trp Ser Asp Asp Thr Asn Pro Leu Phe Asn Gln Tyr Asn Lys Ser Ser

370 375 380

Asn Ile Ala

385

<210> 2

<211> 393

<212> PRT

<213> bacteria of the family of Chinese bacillaceae (Sinobactaceae bacteria)

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Met Leu Lys Lys Ala Arg Leu Ile Ile Asp Leu Gln Phe Gly Ser Thr

1 5 10 15

Gly Lys Gly Leu Ile Ala Gly Tyr Leu Ala Ala Arg His Asn Pro Asp

20 25 30

Thr Leu Ile Thr Ala Trp Ala Ala Asn Ala Gly His Thr Tyr Ile Asp

35 40 45

Ser Glu Gly Thr Lys Phe Val His Thr Met Leu Ala Asn Gly Ile Val

50 55 60

Ser Lys Asn Leu Arg Arg Ile Leu Ile Gly Pro Gly Ser Leu Ile Asn

65 70 75 80

Pro Asp Ala Leu Val Ala Glu Ile Asn Glu Ala Leu Ala Leu Gly Val

85 90 95

Asp Leu Ser Asn Val Lys Leu Val Ile His Pro His Ala Ala Val Ile

100 105 110

Gln Gln Arg His Ile Glu Glu Glu Gln Gly Pro Met Thr Lys Ile Gly

115 120 125

Ser Thr Lys Lys Gly Val Gly Ala Ala Ala Ile His Arg Ile Arg Arg

130 135 140

Asp Pro Asp Asp Asn Asn Val Ala Val Asn Ala Leu Gln Gly His Phe

145 150 155 160

Leu Gly Gln Tyr Val Gly Thr Ile Glu Glu Tyr Asn Glu Gln Leu Asn

165 170 175

Ala Ala Glu Ile Ala Gln Ile Glu Gly Ala Gln Gly Tyr Ser Leu Ser

180 185 190

Met Tyr His Gly Met Tyr Pro Tyr Thr Thr Ser Arg Asp Val Thr Thr

195 200 205

Ala Gln Ile Phe Ala Asp Cys Gly Leu Pro Ile Ser Trp Leu Ala Arg

210 215 220

Thr Glu Val Ile Gly Thr Val Arg Thr Phe Pro Ile Arg Val Ala Asn

225 230 235 240

Arg Phe Asp Glu Gln Gly Thr Gln Ile Gly Tyr Ser Gly Gly Cys Tyr

245 250 255

Pro Asp Gln His Glu Met Ala Trp Pro Glu Leu Gly Leu Glu Ala Glu

260 265 270

Leu Thr Thr Val Thr Lys Leu Pro Arg Arg Ile Phe Ser Leu Ser Phe

275 280 285

Ile Gln Leu Tyr Glu Ala Met Arg Ile Asn Gly Val Asn Lys Leu Phe

290 295 300

Val Asn Phe Ala Asn Tyr Leu Arg Thr Pro Gly Glu Tyr Arg Arg Val

305 310 315 320

Met Asp Gly Ile Gln Ala Val Ala Val Gly Ser Gly Ala Asp Ile Gly

325 330 335

Trp Ile Gly Phe Gly Pro Thr Asp Asp His Val Ile Glu Thr Pro Pro

340 345 350

Glu Leu Val Thr Ala Asn Leu His Ser Asp Arg Leu Met Ala Leu Trp

355 360 365

Gln Ser Thr Asn Val Thr Gly Gly Lys Met Pro Val Pro Ala Gln His

370 375 380

Ala Asp Phe Gly Gln Glu Ser Leu Ala

385 390

<210> 3

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<212> PRT

<213> Salmonella phage PMBT28(Salmonella phase PMBT28)

<400> 3

Met Asn Ser Asn Lys Lys Ala Thr Ile Val Val Asp Ala Gln Phe Gly

1 5 10 15

Ser Thr Gly Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Arg Asp Gln

20 25 30

Pro Asp Val Val Met Thr Ala Trp Ser Ala Asn Ala Gly His Thr Tyr

35 40 45

Ile Asn Ala Glu Gly Arg Lys Phe Val His Cys Met Leu Ala Asn Gly

50 55 60

Ile Val Ser Pro Lys Leu Thr Thr Val Leu Ile Gly Pro Gly Ser Gln

65 70 75 80

Met Asn Ala Glu Leu Leu Arg Asp Glu Ile Leu Ser Cys Ala Asp Leu

85 90 95

Leu Gln Gly Lys Thr Ile Leu Leu His Ala Ser Ala Ala Leu Ile Leu

100 105 110

Gln Lys His Val Glu Glu Glu Ala Gly Pro Met Thr Lys Ile Gly Ser

115 120 125

Thr Lys Lys Gly Cys Gly Ala Ala Met Ile Ala Lys Ile Arg Arg Asn

130 135 140

Pro Asp Asp Asn Asn Thr Val Gly Ala Asn Gly Asp Tyr Met Glu Glu

145 150 155 160

His Ile Tyr Gly Pro Val Arg Glu Ala Gly Val Phe Ile Arg Thr Ala

165 170 175

Thr Asn Ala Glu Tyr Met Ala Val Val Tyr Asp Ala Glu Arg Ile Gln

180 185 190

Val Glu Gly Ala Gln Gly Phe Ser Leu Gly Ile Asn Asn Gly Phe Tyr

195 200 205

Pro Tyr Val Thr Ser Arg Glu Cys Thr Pro Ala Gln Val Ala Val Asp

210 215 220

Val Asn Leu Pro Leu Ala Phe Ile Asp Lys Val Val Ala Cys Met Arg

225 230 235 240

Thr Leu Pro Ile Arg Val Ala Asn Arg Tyr Asn Asp Lys Gly Glu Gln

245 250 255

Ile Gly Trp Ser Gly Pro Cys Tyr Pro Asp Gln Lys Glu Leu Asp Trp

260 265 270

Glu Lys Asp Leu Gly Met Glu Ala Glu Leu Thr Thr Val Thr Lys Leu

275 280 285

Pro Arg Arg Ile Phe Thr Phe Ser Tyr Glu Gln Thr Lys Ala Ala Leu

290 295 300

Glu Val Ile Arg Pro Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu

305 310 315 320

Glu Pro Asp Glu Val Ala Ala Val Ile Gly Thr Ile Glu Arg Ala Ala

325 330 335

His Glu Leu Lys Val Pro Gly Pro Met Pro Leu Ala Arg Tyr Tyr Gly

340 345 350

Tyr Gly Pro Thr Val Asn Asp Ile

355 360

<210> 4

<211> 343

<212> PRT

<213> Vibrio phage phiVC8(Vibrio phage phiVC8)

<400> 4

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Val Pro Glu Leu Thr Thr Val Thr Lys Lys Val Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Glu Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Asn Asp Val

325 330 335

Glu Leu Arg Glu Asp Val Met

340

<210> 5

<211> 203

<212> PRT

<213> Acinetobacter phage SH-Ab15497 (Acinetobacter phase SH-Ab 15497)

<400> 5

Met Asp Lys Leu Asn Ile Arg Asp Ile Leu Arg Ala Gln Asp Val Thr

1 5 10 15

Arg Trp Gln Ile Val Arg Thr Lys Lys Gln Ser Val Ala Glu His Thr

20 25 30

Phe Ala Val Gln Ala Val Leu Met Arg Leu Val Pro Leu Leu Ile Ser

35 40 45

Thr Tyr Thr Ala Pro Met Lys Val Gly Phe Glu Glu Arg Leu Leu Cys

50 55 60

Glu Cys Ile Met Gly Ala Phe Trp His Asp Ile Pro Glu Val Ile Thr

65 70 75 80

Gly Asp Ile Ala Ser Pro Val Lys Arg Leu Ile Arg Asp Gly Gly Asp

85 90 95

Ile Thr Pro Leu Asp Asp Leu Glu Lys Lys Val Asp Pro Ala Phe Ile

100 105 110

Lys Cys Tyr Thr Ala Ala Lys Pro Leu Thr Leu Ala Ile Ile Lys Cys

115 120 125

Ala Asp Leu Met Glu Met Val Tyr His Leu Asn Glu Tyr Gly Asp Gln

130 135 140

Arg Ala Asn Ser His Ser Trp Arg Val Gln His Gly Ile Asn Asn Ala

145 150 155 160

Phe His Glu His Ile His Asn Cys Ser Glu Asn Phe Pro Ala Phe Lys

165 170 175

Trp Asp Val Ala His Gly Leu Leu Ile Glu Met Leu Asp Pro Ser Gln

180 185 190

Glu Thr Asp Ile Asp Ser Ile Val Asn Gly Ile

195 200

<210> 6

<211> 194

<212> PRT

<213> Salmonella phage PMBT28(Salmonella phase PMBT28)

<400> 6

Met Met Thr Met Thr Pro Arg Asp Leu Met Arg Ala Gln Tyr Val Thr

1 5 10 15

Arg Trp Gln Ile Val Pro Thr Thr Arg Ser Gln Ser Val Ala Gln His

20 25 30

Ser Trp Ala Val Ala Met Leu Ala Met Asn Leu Trp Cys Arg Arg Thr

35 40 45

Gly Gly Gln Pro Gly Glu Ala Ala Thr Asp Val Glu Leu Gly Lys Ile

50 55 60

Ala Val Met Ala Leu Trp His Asp Ala Pro Glu Val Phe Thr Gly Asp

65 70 75 80

Ile Asn Thr Pro Thr Lys Ile Phe Leu Asn Ala Ser Asn Ala Leu Asp

85 90 95

Glu Leu Glu Asn Thr Ala Gly Asp Gly Tyr Leu Glu Ser Met Asp Gly

100 105 110

Gly Pro Ile Arg Thr Cys Val Lys Ile Ala Asp Phe Leu Glu Ala Met

115 120 125

Tyr Trp Leu Met Glu His Gly Asp Gly His Tyr Ala Asn Asn Gln Leu

130 135 140

His Gly Leu Asn Glu Arg Phe His Gln Tyr Leu Asn Glu His Ala Pro

145 150 155 160

Leu Trp Arg Asp Ser Ala Val Ala Leu Trp Lys Glu Leu Ser Asp Val

165 170 175

Asn Ala Glu Thr Thr Thr Phe Gln Arg Val Asn Tyr Leu Lys Ala Asn

180 185 190

Asp Ala

<210> 7

<211> 175

<212> PRT

<213> cyanobacterial phage (cyanophage)

<400> 7

Met Thr Leu Gln Ile Thr Glu Thr Tyr Glu Arg Leu Arg Ala Ser His

1 5 10 15

Ile Ser Arg Trp Gly Ile Val Gln Thr Thr Tyr Pro Gln Asn Ile Ala

20 25 30

Glu His Met Trp Arg Val Trp Leu Leu Cys Arg Asp Trp Gly Ala Ala

35 40 45

Ala Gly Met Pro Gln His Thr Val Arg Gln Ala Cys Glu Phe Ala Leu

50 55 60

Val His Asp Leu Ala Glu Ile Arg Thr Gly Asp Ala Pro Thr Pro His

65 70 75 80

Lys Thr Pro Glu Leu Lys Glu Leu Leu Ala Gly Ile Glu Ala Gln Ile

85 90 95

Val Pro Glu Val Ala Glu Leu Glu Ala Thr Met Ala Pro Glu Ala Arg

100 105 110

Glu Leu Trp Lys Phe Cys Asp Thr Ala Glu Ala Val Leu Phe Leu Lys

115 120 125

Val Asn Gly Leu Gly Ala His Ala Tyr Asp Val Gln His Leu Leu Met

130 135 140

Glu Gln Met Lys Arg Arg Leu Met Asp Ser Val Leu Asp Val Glu Val

145 150 155 160

Gln Asp Glu Leu Met Phe Gln Phe Glu Arg Thr Ile Lys Lys Thr

165 170 175

<210> 8

<211> 385

<212> PRT

<213> Acinetobacter phage SH-Ab15497 (Acinetobacter phase SH-Ab 15497)

<400> 8

Met Ser Gly Asn Lys Phe Asp Gln Glu Lys Val Asp Leu His Val Leu

1 5 10 15

Asp Pro Phe Phe Ile Glu Gly Thr Ala Arg Val Ala Gln Phe Gly Glu

20 25 30

Gln Lys Tyr Gly Arg Ser Asn Trp Met Gln Gly Leu Thr Gln Thr Arg

35 40 45

Ile Ile Asn Ala Ile Lys Arg His Ile Ala Gln Ile Glu Lys Gly Glu

50 55 60

Asp Ile Asp Glu Glu Ser Gly Phe His His Ala Tyr His Ala Ala Trp

65 70 75 80

Gly Cys Gln Val Leu Ala Tyr Gln His Arg Asn Gly Gln Thr His Leu

85 90 95

Asp Asp Arg Arg Trp Ser Glu Ser Val Arg Asp Ala Asp Thr Lys Ile

100 105 110

Gly Thr Cys Glu Gly Ile Ser Gly His Thr Val Pro Cys Met Tyr Glu

115 120 125

Gly Pro Phe Gly Arg Leu His Pro Val Asp Gly Glu Lys Asp Gly Leu

130 135 140

Val Met Ser Phe Val Gln Ser Glu Ala Asp Glu Gly Thr Ala Gln Gly

145 150 155 160

Asp Pro Ile Gln Gln Leu Gln Gln Met Ile Ser Glu Trp Ala Asp Gln

165 170 175

Val Tyr Pro Asp Arg Thr Val Glu Asn Ala Leu Thr Lys Met Met Leu

180 185 190

His Glu Ile Pro Glu Leu Leu His Gly Lys Ala Met Asp Pro Ala Glu

195 200 205

Phe Ala Asp Val Ala Ile Leu Leu Phe Asp Val Ala His Leu Gln Gly

210 215 220

Ile Asp Ile Ala Gln Ala Met Arg Glu Lys Met Glu Ile Asn Gln Ala

225 230 235 240

Arg Asp Trp Lys Ile Asp Pro Ala Thr Gly Leu Met Ser His Val Lys

245 250 255

Pro Lys Gly Met Met Glu Thr Ile Arg Asp Ala Val Gln Gly Ile Gly

260 265 270

Asp Ala Ala Arg Ile Met Ala Ala Pro Ser Arg Leu Leu Asn Gly Asn

275 280 285

Asn Met Glu Leu Ala Glu Tyr Thr Ala Glu Thr Leu Pro Lys Pro Pro

290 295 300

Glu Lys Pro Trp Glu Ile Thr Ile Pro Asn Trp Ala Leu Lys Thr Glu

305 310 315 320

Glu Gly Thr His Ile Lys Leu Arg Ala Gly Ser Gly Val Phe Gly Arg

325 330 335

Val Lys Tyr Gln Ser Gln Cys Ile Leu Met His Lys Asn Met Arg Lys

340 345 350

Arg Ser His Leu Glu Thr Tyr Tyr Cys Ala Thr Ile Lys Asp Thr Val

355 360 365

Thr Glu Asp Glu Tyr Asn Val Pro Trp Ser Glu Ile Glu Pro Trp Thr

370 375 380

Asn

385

<210> 9

<211> 343

<212> PRT

<213> Vibrio phage JSF15(Vibrio phase JSF15)

<400> 9

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Val Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Phe Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Asp Val Met

340

<210> 10

<211> 343

<212> PRT

<213> Vibrio phage JSF33(Vibrio phase JSF33)

<400> 10

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Gly Gln Leu Gly

245 250 255

Gln Thr Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Glu Met Met

340

<210> 11

<211> 343

<212> PRT

<213> Vibrio phage JSF9(Vibrio phase JSF9)

<400> 11

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Thr Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Glu Met Met

340

<210> 12

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Temper16(Arthrobacter phage Temper16)

<400> 12

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Arg Glu Ala Ala Arg His Asn

20 25 30

His Ser Ile Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Lys Gly His

85 90 95

Gly His Ile Leu Gln Leu Leu Val Asp Glu Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ser Glu Gly Gln Met Val Asp Arg Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Gln Leu Leu

145 150 155 160

Thr Glu Ile Ser Gly Val Lys Val Cys Asp Thr Val Ala Tyr Leu His

165 170 175

Gly Gln Ala Ser Arg Glu Glu Val Asn Ile Ile Val Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Ala Ala Val Gln Val Met Ile Ala Cys Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Glu Gly Glu Thr

245 250 255

Thr Trp Glu Glu Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Ala Ala Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Lys Ile Asp Glu Asp Asp Ile His Gly

290 295 300

Gln Leu Gln Leu Leu Val Ser Gly Gly Pro Lys Val Thr Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Val Pro Gly Ile Glu Gly Ala Thr Asp Ile

325 330 335

Asp Lys Ile Glu Pro Glu Glu Phe Ala Lys Val Glu Glu Trp Ile Glu

340 345 350

Lys Ile Tyr Arg Glu Thr Gly Ala His Thr Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Leu Leu Ile Gly Ala

370 375

<210> 13

<211> 379

<212> PRT

<213> Arthrobacter phage Christian (Arthrobacter phase Christian)

<400> 13

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys

20 25 30

Ser Asp Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu

85 90 95

Asp His Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu

115 120 125

Ser Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Val Trp Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr

165 170 175

Leu His Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn

245 250 255

Glu Thr Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala

275 280 285

Asp Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu

290 295 300

Glu Ala Leu Leu Trp Gln Ala Val Gln Glu Gly Pro His Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Ser

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp

340 345 350

Ile Asp Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 14

<211> 343

<212> PRT

<213> Vibrio phage Rosov 6(Vibrio phase Rosov 6)

<400> 14

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Thr Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Glu Met Met

340

<210> 15

<211> 389

<212> PRT

<213> Arthrobacter bacteriophage Sergei (Arthrobacter phage Sergei)

<400> 15

Met Lys Arg Asp Asn Pro Asn Arg Lys Glu Asn Lys Leu Ser Asn Val

1 5 10 15

Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala Lys Gly His Val

20 25 30

Thr Ala Gln Leu Val Arg Glu Ala Ala Arg His Asn His Ser Ile Val

35 40 45

Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Ala Tyr Asp Asp

50 55 60

Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val Gly Ala Val Ile

65 70 75 80

Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu Ile Asp Leu Pro

85 90 95

Val Leu Leu Asp Glu Ile His Leu Ala Lys Gly His Gly His Ile Leu

100 105 110

Gln Leu Leu Val Asp Glu Asn Ala Thr Met Ile Glu Tyr His His Lys

115 120 125

Met Gln Glu Ser Glu Gly Gln Met Val Asp Arg Ile Gly Ser Thr Ala

130 135 140

Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp Arg Lys Ala Arg

145 150 155 160

Arg Leu Arg Asp Val Pro Glu Ala Val Gln Leu Leu Thr Glu Ile Ser

165 170 175

Gly Val Lys Val Cys Asp Thr Val Ala Tyr Leu His Gly Gln Ala Ser

180 185 190

Arg Glu Glu Val Asn Ile Ile Val Glu Gly Thr Gln Gly Tyr Gly Leu

195 200 205

Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser Ser Asp Cys Arg

210 215 220

Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro Trp His Pro Gly

225 230 235 240

Ile Ala Ala Val Gln Val Met Ile Ala Cys Arg Val Tyr Pro Ile Arg

245 250 255

Val Ala Gly Asn Ser Gly Pro Met Glu Gly Glu Thr Thr Trp Glu Glu

260 265 270

Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg

275 280 285

Val Gly Ala Trp Asp Ala Ala Leu Val Lys Ala Ala Phe Glu Ala Asn

290 295 300

Gly Gly Val Lys Ile Asp Glu Asp Asp Ile His Gly Gln Leu Gln Leu

305 310 315 320

Leu Val Ser Gly Gly Pro Lys Val Thr Val Ala Leu Thr Met Leu Asp

325 330 335

Gln Val Val Pro Gly Ile Glu Gly Ala Thr Asp Ile Asp Lys Ile Glu

340 345 350

Pro Glu Glu Phe Ala Lys Val Glu Glu Trp Ile Glu Lys Ile Tyr Arg

355 360 365

Glu Thr Gly Ala His Thr Ala Met Ile Thr Thr Ser Pro Lys Thr Ala

370 375 380

Leu Leu Ile Gly Ala

385

<210> 16

<211> 376

<212> PRT

<213> Long-tailed bacteriophages family (Siphoviridae sp.)

<400> 16

Met Lys Ser Arg Thr Ala Thr Leu Ile Cys Asp Leu Gln Phe Gly Ser

1 5 10 15

Thr Gly Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Arg Asp Lys Pro

20 25 30

Asp Thr Val Ile Thr Ala Trp Ser Ala Asn Ala Gly His Thr Tyr Ile

35 40 45

Asp Arg Ala Gly Arg Lys Tyr Val His Cys Met Leu Ala Asn Gly Ile

50 55 60

Val Ser Pro Asn Leu Lys Gln Val Leu Ile Gly Pro Gly Ser Gln Leu

65 70 75 80

Asp Leu Cys Lys Leu Lys Arg Glu Ile Glu Glu Cys Lys Asp Ile Leu

85 90 95

Leu Asp Arg Gly Ala Val Ile Tyr Ile His Gly Ser Ala Cys Val Ile

100 105 110

Ser Glu Arg His Ile Gln Glu Glu Ala Gly Pro Met Thr Lys Ile Gly

115 120 125

Ser Thr Lys Lys Gly Cys Gly Ala Ala Leu Ile Glu Lys Ile Arg Arg

130 135 140

Asn Pro Glu Gly Lys Ala Ile Thr Ile Gly Gln Phe Ala Glu Lys Trp

145 150 155 160

Glu Asn Met Trp Ser Glu Thr Glu Ala Asn Lys Asn Val Arg Cys Glu

165 170 175

Asp Trp Ile Thr Pro Asp Ile Pro Cys Tyr Ile Val Asp Asn Ala Gly

180 185 190

Trp Gln Gln Cys Leu Leu Glu Ala Glu His Ile Gln Ile Glu Gly Ala

195 200 205

Gln Gly Tyr Ser Leu Gly Leu Asn Ser Gly Phe Tyr Pro Tyr Val Thr

210 215 220

Ser Arg Glu Cys Thr Pro Ala Gln Ile Val Ser Asp Cys Ala Phe Pro

225 230 235 240

Met Gln Trp Val Thr Lys Val Val Gly Thr Met Arg Thr Tyr Pro Ile

245 250 255

Arg Val Ala Asn Arg Tyr Asp Ala Glu Gly Asn Met Val Gly Tyr Ser

260 265 270

Gly Pro Gly Tyr Asp Asp Gln Lys Glu Thr Thr Phe Glu Glu Leu Gly

275 280 285

Gln Ala Thr Glu Leu Thr Thr Val Thr Arg Leu Pro Arg Arg Ile Phe

290 295 300

Thr Phe Ser Gln Glu Gln Thr Arg Gln Ala Leu Met Thr Val Arg Pro

305 310 315 320

Asp Glu Ile Phe Leu Asn Phe Val Asn Tyr Cys Asp Asp Gln Thr Leu

325 330 335

Gly Phe Ile Ile Asn Gln Ile Tyr Gly Ala Ala Ile Asp Ala Gly Ile

340 345 350

Pro Tyr Ser Pro Leu Arg Tyr Ile Gly Arg Gly Pro Ala Val Gln Asp

355 360 365

Val Leu Ser Leu Val Glu Asp Cys

370 375

<210> 17

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Urla (Arthrobacter phase Urla)

<400> 17

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Ile Thr Ala Gln Leu Val Lys Gln Ala Val Lys Ser Gly

20 25 30

Arg Gln Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Val Lys Tyr Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Glu Glu Ile His Phe Ala Arg Asp Asn

85 90 95

Gly His Ile Val Gln Leu Leu Val Asp Trp Asn Ala Thr Met Ile Gln

100 105 110

His His His Lys Met Gln Glu Ser Glu Gly Lys Met Val Glu Ser Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp

130 135 140

Arg Lys Ala Lys Arg Leu Ile Asp Phe Pro Glu Ala Cys Asn Leu Leu

145 150 155 160

Gln Glu Ile Pro Gly Val Gln Val Val Asp Thr Val Lys Tyr Leu His

165 170 175

Gly Glu Ser Ser Arg Ser Ser Val Ser Ile Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Glu Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Glu Ser Thr Gln Val Ile Ile Ala Thr Arg Val

225 230 235 240

Phe Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Glu Gly Glu Thr

245 250 255

Ser Trp Glu Glu Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Gln Trp Asp Gly Lys Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Trp Ala Ile Ala Asp Asp Asp Met Glu Gly

290 295 300

Gln Leu Met Gln Met Val Ser Gly Gly Pro Lys Val Val Val Gly Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Thr Thr Phe

325 330 335

Asp Asp Leu Asp Glu Pro Thr Leu Ala Lys Val Glu Glu Trp Ile Asn

340 345 350

Lys Val Tyr Arg Glu Thr Gly Ala His Thr Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Val Leu Phe Gly Val

370 375

<210> 18

<211> 379

<212> PRT

<213> Arthrobacter bacteriophage Megannoll (Arthrobacter phage Megannoll)

<400> 18

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser

20 25 30

Ala Asp Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu

85 90 95

Asp His Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Ile Trp Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr

165 170 175

Leu Tyr Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn

245 250 255

Glu Thr Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala

275 280 285

Asp Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu

290 295 300

Glu Ala Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp

340 345 350

Ile Asp Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 19

<211> 387

<212> PRT

<213> Acinetobacter phage SH-Ab15497 (Acinetobacter phase SH-Ab 15497)

<400> 19

Met Lys Lys Ala Thr Val Ile Cys Asp Met Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Phe Leu Ala Glu Arg Asp Gln Pro Asp Val

20 25 30

Val Val Thr Ala Trp Ser Ala Asn Ala Gly His Thr Tyr Ile Asn Arg

35 40 45

Glu Gly Arg Lys Trp Val His Cys Met Leu Ala Asn Gly Ile Val Ser

50 55 60

Pro Lys Leu Lys Ala Val Leu Ile Gly Gly Gly Ser Gln Met Ser Ile

65 70 75 80

Pro Thr Leu Ile Ser Glu Ile Met Gly Ser Leu Asp Ile Leu Gln Gly

85 90 95

Lys Ser Ile Leu Ile His Glu Asn Ala Cys Ile Ile Gln Gln Arg His

100 105 110

Val Glu Glu Glu Ala Gly Pro Met Thr Lys Ile Gly Ser Thr Lys Lys

115 120 125

Gly Cys Gly Ala Ala Met Met Glu Lys Ile Arg Arg Asn Pro Glu Ser

130 135 140

Lys Ile Val Ala Lys Asp Phe Ile Asp Asp Gly Leu Glu Ile Pro Asp

145 150 155 160

Phe Lys Leu Asp Gly Thr Val Gly Phe Lys Asp Ile Ser Arg His Phe

165 170 175

Glu Glu Leu Gly Val Cys Ile Lys Val Val Ser Asn Glu Val Tyr Leu

180 185 190

Ala Val Leu His Lys Ala Glu Arg Val Gln Val Glu Gly Ala Gln Gly

195 200 205

Phe Ser Leu Gly Leu His Asn Gly Phe Tyr Pro Tyr Val Thr Ser Arg

210 215 220

Glu Cys Thr Pro Ala Gln Ile Cys Ser Asp Cys Asn Val Pro Ile Ser

225 230 235 240

Met Val Asp Lys Val Val Gly Thr Met Arg Thr Tyr Pro Ile Arg Val

245 250 255

Ala Asn Arg Phe Asp Asp Glu Gly Lys Met Val Gly Trp Ser Gly Pro

260 265 270

Cys Tyr Ser Asp Gln Thr Glu Leu Thr Trp Glu Gln Met Gly Val Thr

275 280 285

Pro Glu Lys Thr Thr Val Thr Lys Leu Thr Arg Arg Ile Phe Ser Phe

290 295 300

Ser Arg Met Gln Thr Arg Gln Ala Met Leu Val Cys Met Pro Asp Glu

305 310 315 320

Ile Phe Leu Asn Phe Ala Asn Tyr Cys Ala Ser Glu Asp Glu Leu Ala

325 330 335

Ser Ile Ile Glu Val Ile Ser Asn Glu Gly Gly Asp Val Ser Tyr Ile

340 345 350

Gly Trp Gly Asp Ser Ala Ala His Ile Glu Thr Thr Leu Glu Gly Asp

355 360 365

Trp Ser Asp Asp Thr Asn Pro Leu Phe Asn Gln Tyr Asn Lys Ser Ser

370 375 380

Asn Ile Ala

385

<210> 20

<211> 367

<212> PRT

<213> Salmonella phage PMBT28(Salmonella phase PMBT28)

<400> 20

Met Asn Ser Asn Lys Lys Ala Thr Ile Val Val Asp Ala Gln Phe Gly

1 5 10 15

Ser Thr Gly Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Arg Asp Gln

20 25 30

Pro Asp Val Val Met Thr Ala Trp Ser Ala Asn Ala Gly His Thr Tyr

35 40 45

Ile Asn Ala Glu Gly Arg Lys Phe Val His Cys Met Leu Ala Asn Gly

50 55 60

Ile Val Ser Pro Lys Leu Thr Thr Val Leu Ile Gly Pro Gly Ser Gln

65 70 75 80

Met Asn Ala Glu Leu Leu Arg Asp Glu Ile Leu Ser Cys Ala Asp Leu

85 90 95

Leu Gln Gly Lys Thr Ile Leu Leu His Ala Ser Ala Ala Leu Ile Leu

100 105 110

Gln Lys His Val Glu Glu Glu Ala Gly Pro Met Thr Lys Ile Gly Ser

115 120 125

Thr Lys Lys Gly Cys Gly Ala Ala Met Ile Ala Lys Ile Arg Arg Asn

130 135 140

Pro Asp Asp Asn Asn Thr Val Gly Ala Asn Gly Asp Tyr Met Glu Glu

145 150 155 160

His Ile Tyr Gly Pro Val Arg Glu Ala Gly Val Phe Ile Arg Thr Ala

165 170 175

Thr Asn Ala Glu Tyr Met Ala Val Val Tyr Asp Ala Glu Arg Ile Gln

180 185 190

Val Glu Gly Ala Gln Gly Phe Ser Leu Gly Ile Asn Asn Gly Phe Tyr

195 200 205

Pro Tyr Val Thr Ser Arg Glu Cys Thr Pro Ala Gln Val Ala Val Asp

210 215 220

Val Asn Leu Pro Leu Ala Phe Ile Asp Lys Val Val Ala Cys Met Arg

225 230 235 240

Thr Leu Pro Ile Arg Val Ala Asn Arg Tyr Asn Asp Lys Gly Glu Gln

245 250 255

Ile Gly Trp Ser Gly Pro Cys Tyr Pro Asp Gln Lys Glu Leu Asp Trp

260 265 270

Glu Lys Asp Leu Gly Met Glu Ala Glu Leu Thr Thr Val Thr Lys Leu

275 280 285

Pro Arg Arg Ile Phe Thr Phe Ser Tyr Glu Gln Thr Lys Ala Ala Leu

290 295 300

Glu Val Ile Arg Pro Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu

305 310 315 320

Glu Pro Asp Glu Val Ala Ala Val Ile Gly Thr Ile Glu Arg Ala Ala

325 330 335

His Glu Leu Lys Val Pro Gly Pro Met Pro Leu Ala Arg Tyr Tyr Gly

340 345 350

Tyr Gly Pro Thr Val Asn Asp Ile Asp Leu Asp Met Arg His Gln

355 360 365

<210> 21

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Carpal (Arthrobacter phase Carpal)

<400> 21

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 22

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage CallieOMalley (Arthrobacter phage CallieOMalley)

<400> 22

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Lys Leu Ala Val Lys Ala Glu

20 25 30

Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly His Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Asp Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp Gln

85 90 95

Gly His Ile Leu Asp Leu Leu Ile Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Leu Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val Val Asp Thr Val Asp Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Ser Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Ile Leu Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu His Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Glu Leu Val Ala Glu Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Gly Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Glu Ala Val Gln Gly Gly Pro Ser Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Glu Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Glu

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 23

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Bodacious (Arthrobacter phase Bodacious)

<400> 23

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys Ser Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Ser Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 24

<211> 377

<212> PRT

<213> Arthrobacter phage Moki (Arthrobacter phase Moki)

<400> 24

Met Ser Asn Val Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Val Lys Ala Glu

20 25 30

Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp Asn

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Ala Ala Leu Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val Val Asp Thr Val Glu Tyr Leu His

165 170 175

Gly Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Ile Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Met Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Glu Ala Thr Leu Gln Lys Val Glu Ala Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 25

<211> 406

<212> PRT

<213> Microbacterium phage Goodman (Microbacterium phase Goodman)

<400> 25

Met Gln Phe Ile Asp Thr Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Lys Ala Ala Ala Lys Asp Ala

20 25 30

Arg Asp Tyr Ala Thr Glu His Asp Val Pro Ile Pro Glu Thr Ile Asn

35 40 45

Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp Asp Gln

50 55 60

Gly Gln Lys Phe Ala Leu Arg Gln Ile Pro Val Gly Ala Val Tyr Glu

65 70 75 80

Asp Val Lys Leu Tyr Ile Ala Pro Gly Ser Glu Ile Asp Leu Asp Val

85 90 95

Leu Tyr Ser Glu Ile Glu Ala Leu Glu Ala Ala Gly His Pro Ile Gln

100 105 110

His Arg Leu Trp Ile Ser Arg Gln Ala Thr Val Ile Thr Gln Glu His

115 120 125

Lys Asp Ala Glu Ala Ala Leu Val Gly Lys Ile Gly Ser Thr Gly Lys

130 135 140

Gly Ile Gly Ala Ala Arg Ala Ala Arg Leu Leu Arg Ser Ala Gln Thr

145 150 155 160

Ile Gly Asp Tyr Met Glu Asp Ala Gly Leu Gly Thr Met Trp Glu Trp

165 170 175

Arg Glu Pro Ser Glu Trp Tyr Ala Ser Asp Asp Phe Val His Asp Asn

180 185 190

Leu Ser His Val Leu Ile Glu Gly Thr Gln Gly Tyr Gly Leu Ser Leu

195 200 205

Arg Ala Ser Gly Asn Tyr Pro Tyr Val Thr Ser Ser Asp Ala Arg Ala

210 215 220

Ile Asp Phe Met Ala Met Ala Gly Val Asp Pro Thr Arg Cys Ser Val

225 230 235 240

Lys Ala Thr Asn Trp Val Val Ala Arg Val Phe Pro Ile Arg Val Ala

245 250 255

Gly Asn Ser Gly His Met Lys Gly Glu Thr Ser Trp Asp Glu Leu Gly

260 265 270

Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg Val Gly

275 280 285

Glu Phe Asp Val Asp Leu Leu Arg Glu Ala Val Gln Ala Asn Gly Gly

290 295 300

His Asn Ala Gln Val Val Ile Thr Met Leu Asp Gln Val Ile Pro Gly

305 310 315 320

Leu Ala Asp Val Asp Pro Asp Gln Ile His Asp Asp Glu Gly Thr Val

325 330 335

Asp Pro Ser Gln Ser Glu Tyr Leu Gln Glu Ala Leu Glu Trp Val Asn

340 345 350

Glu His Ala Gly Tyr Asp Lys Ile Gly Ala His Val Gly Ala Ile Thr

355 360 365

Phe Gly Pro Thr Lys Met Leu Phe Thr Asn His Gly Ala Asn Ala Asn

370 375 380

Asn Pro Glu Gly Gly Asp Gln Ala Met Val Asp Ala Ile Met Ser Gln

385 390 395 400

Ile Phe Gly Gly Arg Glu

405

<210> 26

<211> 371

<212> PRT

<213> Streptomyces phage Hiyaa (Streptomyces phage Hiyaa)

<400> 26

Met Gly Gly Lys Leu Leu Val Val Ala Gly Ala Gln Tyr Gly Ser Glu

1 5 10 15

Ala Lys Gly His Val Ala Asp Gln Leu Ser Arg Pro Ala Val Ala Ser

20 25 30

Asp Asn Val Val Val Met Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Val Tyr Gly Leu Cys Pro Asn Asp Cys Thr Pro Asp Asp Ser His Met

50 55 60

Ser Gly Glu Asn Trp Ile Gly His Pro Trp Arg Leu Arg Thr Val Pro

65 70 75 80

Val Gly Ala Val Ser Asn Pro Asp Ala Asp Leu Val Ile Ala Ala Gly

85 90 95

Ser Glu Ile Asp Tyr Asn Val Leu Met Ser Glu Val Val Ala Leu Asp

100 105 110

Ala Ala Gly Tyr Lys Val Ser Gln Arg Leu Val Ile Asp Thr Gln Ala

115 120 125

Thr Leu Leu Glu Pro Arg His Ile Gln Glu Glu Val Asp Ala Lys Ile

130 135 140

Gln Glu Arg Leu Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala

145 150 155 160

Asp Arg Ile Trp Arg Leu Ala Lys Thr Trp Gly Asp His Ile Gln Asp

165 170 175

Glu Gly Arg Ile Glu Ser Ala Glu Phe Val Arg Gly Arg Leu Ala Asp

180 185 190

Gly Ala Thr Val Val Ile Glu Gly Thr Gln Gly Phe Gly Leu Gly Leu

195 200 205

His Ala Gly His Tyr Pro Gln Cys Thr Ser Ser Asp Cys Arg Ala Ile

210 215 220

Asp Phe Leu Ser Met Ala Gly Leu Ser Pro Trp Met Arg Glu Val Asp

225 230 235 240

Glu Phe Gly Val Trp Leu Ala Ala Arg Val Arg Pro Ile Arg Val Ala

245 250 255

Gly Asn Ser Gly Pro Met Lys Asn Glu Thr Thr Trp Gln Asp Leu Arg

260 265 270

Leu Pro Glu Glu Tyr Thr Thr Val Thr Lys Lys Val Arg Arg Val Gly

275 280 285

Glu Trp Asp Gly Glu Leu Val Ala Arg Ala Val Ile Ala Asn Gly Gly

290 295 300

Ala Pro Ala Val Arg Val Ala Leu Thr Met Val Asp Ser Ile Phe Asp

305 310 315 320

Glu Ile Arg Asn Ala Glu Gly Met Phe Asp Asp Val Asp Trp Thr His

325 330 335

Glu Val Ala Pro Pro Leu Pro Lys Ile Val Thr Asn Ile Glu Arg Glu

340 345 350

Ile Gly Ala Pro Ile Arg Met Ile Thr Thr Ser Pro Thr Thr Ala Leu

355 360 365

Trp Arg Pro

370

<210> 27

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage ChewChew (Arthrobacter phage ChewChew)

<400> 27

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys Ser Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 28

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Huckleberry (Arthrobacter phage Huckleberry)

<400> 28

Met Ser Asn Val Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Val Lys Gly Glu

20 25 30

Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp Asn

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Ala Ala Leu Glu Leu Leu

145 150 155 160

Asn Gln Phe Pro Gly Val Arg Val Val Asp Thr Val Glu Tyr Leu His

165 170 175

Gly Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Asn Glu Glu Asn Leu Glu Ala

290 295 300

Leu Leu Trp Glu Ala Val Gln Gly Gly Pro Ser Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Asp Glu Ala Thr Leu Gln Lys Val Glu Ala Trp Met Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 29

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Lennox (Arthrobacter phage Lennox)

<400> 29

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys Ser Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Gln Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 30

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage BigMack (Arthrobacter phase BigMack)

<400> 30

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Asp Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Ala Ala Leu Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val Val Asp Thr Val Glu Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 31

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Beethoven (Arthrobacter phage Beethoven)

<400> 31

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Ser Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 32

<211> 341

<212> PRT

<213> Streptomyces phage ZP6(Alteromonas phage ZP6)

<400> 32

Met Asn Val Lys Met Ile Val Asp Leu Gln Phe Gly Ser Thr Gly Lys

1 5 10 15

Gly Leu Ile Ala Gly Tyr Leu Ala Glu Arg Asp Gln Pro Asp Cys Val

20 25 30

Val Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Asp Glu

35 40 45

Gly Arg Thr Trp Ile His Lys Val Leu Pro Asn Gly Ile Val Ser Pro

50 55 60

Lys Leu Lys Tyr Val Met Ile Gly Pro Gln Ser Val Phe Ser Leu Glu

65 70 75 80

Gln Leu Arg Lys Glu Tyr Lys Glu Ser Phe Asp Leu Met Ser Lys Val

85 90 95

Gly Leu Ile Ile His Glu Ser Ala Val Val Leu Gln Asp Ile His Arg

100 105 110

Glu Val Glu Gln Gln Ala Leu Ser Gly Ile Ser Ser Thr Met Gln Gly

115 120 125

Ser Ala Ala Ala Thr Val Glu Lys Met Met Arg Asn Pro Asn Arg Asp

130 135 140

Ser Arg Ala Lys Thr Val Leu Lys Gly Thr Glu Phe Glu Glu Cys Val

145 150 155 160

Thr Asp His Arg Ala Tyr Gln Thr Ile Met Gln Gly Cys Asp Arg Ile

165 170 175

Gln Ala Glu Ala Ala Gln Gly Tyr Ser Leu Gly Leu Asn Ala Gly Phe

180 185 190

Trp Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro Gln Arg Phe Leu Ala

195 200 205

Asp Met Gly Ile Pro Leu Leu Asn Leu Asp Leu His Val Val Gly Thr

210 215 220

Ala Arg Val His Pro Ile Arg Val Gly Asn Thr Pro Asp Gly Tyr Ser

225 230 235 240

Gly Asp Trp Tyr Pro Asp Gln Glu Glu Ile Thr Trp Glu Ser Ile Gly

245 250 255

Gln Lys Ala Glu Leu Thr Thr Val Thr Lys Arg Ala Arg Arg Ile Ala

260 265 270

Thr Trp Ser Trp Leu Gln Ile Thr Asp Ala Leu Asn Asp Cys Ala Pro

275 280 285

Asp Glu Ile Phe Leu Asn Phe Cys Asn Tyr Asp Thr Asp Gln Ala Val

290 295 300

Asp Ile Ala Ser Lys Leu Pro Glu Ile Ala Tyr Met Gly Tyr Gly Pro

305 310 315 320

Ala Arg Gln Asp Ile Ala Glu Val Ala Asn His Gly Gly Gln Ile Thr

325 330 335

Val Leu Gly Gln Ile

340

<210> 33

<211> 377

<212> PRT

<213> Arthrobacter phage Savage2526(Arthrobacter phage Savage2526)

<400> 33

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Thr Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Ala His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 34

<211> 377

<212> PRT

<213> Arthrobacter phage TattModd (Arthrobacter phage TattModd)

<400> 34

Met Ser Asn Ile Ala Cys Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 35

<211> 377

<212> PRT

<213> Arthrobacter phage HeadNerd (Arthrobacter phase HeadNerd)

<400> 35

Met Ser Asn Val Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Val Lys Ala Glu

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp Asn

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Ala Ala Leu Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val Val Asp Thr Val Glu Tyr Leu His

165 170 175

Gly Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Ile Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Gln Gly Gly Pro Ser Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 36

<211> 373

<212> PRT

<213> Bacillus phage vB _ BpsS-140(Bacillus phage vB _ BpsS-140)

<400> 36

Met Ile Ser Gln Thr Ile His Ser Arg Glu Arg Asp Ser Met Thr Ala

1 5 10 15

Lys Val Thr Ala Val Leu Gly Gly Gln Val Gly Ser Glu Gly Lys Gly

20 25 30

Lys Phe Val Gly Tyr Leu Ala Arg His Asp Gln Phe Asn Thr Ala Ile

35 40 45

Cys His Phe Met Ser Asn Ala Gly His Ser Trp Val Asn Asp Glu Gly

50 55 60

Asp Lys Ile Ile Val Gln Gln Leu Pro Met Ala Val Val Asn Pro Asn

65 70 75 80

Ala Leu Leu Met Ile Gly Ala Gly Ser Ala Phe Asp Ile Asp Ile Leu

85 90 95

Val Ser Glu Leu Asn Lys Tyr Asp Ala Trp Asn Arg Val Val Ile His

100 105 110

Pro Arg Ala Met Val Ile Glu Gln Arg His Lys Asp Gln Glu Ala Ile

115 120 125

Ser Leu Asn Arg Ile Ser Ser Thr Leu Lys Gly Cys Gly Phe Ala Ser

130 135 140

Ala Asp Lys Ile Thr Arg Gly Glu Asn Val Thr Leu Ala Lys Asp Leu

145 150 155 160

Lys Cys Arg Leu Ser Ala Leu Val Ala Pro Thr Pro Ala Leu Phe Glu

165 170 175

His Ile Leu His Glu Glu Ser Arg Val Leu Leu Glu Val Ala Gln Gly

180 185 190

Tyr Asp Leu Asp Ile Asn His Gly Val Glu Tyr Pro Tyr Cys Thr Ser

195 200 205

Arg Gln Thr Thr Val Thr Gln Ser Leu Ala Asp Ser Ala Leu Pro Pro

210 215 220

Gln Ser Ile Asp Glu Val Ile Ala Val Ile Arg Pro Tyr Pro Ile Arg

225 230 235 240

Val Gly Asn Ala Tyr Asp Lys Asp Gly Asn Met Ile Gly Thr Ser Gly

245 250 255

Ser Tyr Pro Ser Arg Glu Ile Asp Trp Asp Thr Val Ala Met Arg Ala

260 265 270

Gly Met Pro Arg Glu Glu Ile Thr Glu Phe Ala Thr Val Thr Gly Lys

275 280 285

Leu Arg Arg Val Phe Glu Phe Asp Met Asp Arg Ile Val Lys Met Val

290 295 300

Arg Ser Asn Gly Val Thr Gln Ile Ala Leu Asn Phe Ala Asn Tyr Ile

305 310 315 320

Asp Tyr Lys Val Gln Gly Ala Thr Arg Ile Glu Asp Ile Thr Pro Lys

325 330 335

Val Trp Ala Phe Ile His Glu Ile Glu Leu Ala Thr Gly Val Arg Val

340 345 350

Thr Leu Ile Gly Thr Gly Ala Lys Asp Asn Glu Ile Val Asp Leu Arg

355 360 365

Gly Thr Thr Ala Arg

370

<210> 37

<211> 379

<212> PRT

<213> Arthrobacter bacteriophages Litotes (Arthrobacter phage Litotes)

<400> 37

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Lys Leu Ala Val Lys

20 25 30

Ala Glu Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly His Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Asp Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu

85 90 95

Asp Gln Gly His Ile Leu Asp Leu Leu Ile Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Lys Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Ile Trp Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Leu Ala

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Arg Val Val Asp Thr Val Asp Tyr

165 170 175

Leu His Thr Ala Leu Gln Lys Pro Ser Val His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Ile Leu Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Asn

245 250 255

Glu Thr Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu His Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Glu Leu Val Ala

275 280 285

Glu Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Gly Glu Asp Asn Leu

290 295 300

Glu Ala Leu Leu Trp Glu Ala Val Gln Gly Gly Pro Ser Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Glu

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp

340 345 350

Ile Glu Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 38

<211> 377

<212> PRT

<213> Arthrobacter phage OurGirlNesie (Arthrobacter phase OurGirlNesie)

<400> 38

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys Ser Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Ser Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Thr

370 375

<210> 39

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Pterodylyl (Arthrobacter phase Pterodylyl)

<400> 39

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys Ser Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Glu Ala Val Gln Gly Gly Pro Ser Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Lys Pro Glu Thr Leu Gln Lys Val Glu Ala Trp Leu Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 40

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage riverdale (Arthrobacter phage riverdale)

<400> 40

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Thr Asp

20 25 30

Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 41

<211> 418

<212> PRT

<213> Microbacterium phage Theresta (Microbacterium phage Theresta)

<400> 41

Met Thr Thr Met Val Asp Val Val Val Gly Gly Gln Tyr Gly Ser Glu

1 5 10 15

Ala Lys Gly His Val Thr Ala Gln Leu Val Thr Gln Ala Ala His Glu

20 25 30

Arg Asp Ser Glu Gln Gly Asn His Phe Gly Ile Asp Val Trp Asn Ile

35 40 45

Arg Val Ala Gly Pro Asn Ala Gly His Thr Ala Tyr Asp Ser Glu Gly

50 55 60

Arg Lys Phe Ala Phe Arg Thr Leu Pro Ile Gly Ala Val Ile Asp Asp

65 70 75 80

Lys Thr Gln Leu Tyr Ile Ala Pro Gly Ser Glu Ile Asp Leu Pro Val

85 90 95

Leu Tyr Lys Glu Ile Gln Glu Ala Glu Ala Ala Gly His Ile Val Arg

100 105 110

Gly Arg Leu Tyr Met Ser Arg Gln Ala Thr Leu Ile Glu Asp Gly His

115 120 125

Lys Leu Val Glu Gln Gly Ala Asp Leu Val Gly Lys Val Gly Ser Thr

130 135 140

Gly Lys Gly Ile Gly Ala Ala Arg Ala Asp Arg Ile Met Arg Thr Ala

145 150 155 160

Ser Leu Val Pro Asp Ala Phe Thr Asp Gly Pro Asp Gly Asp Leu Gln

165 170 175

Ser Gln Pro Trp Ala Trp Ala Glu Pro Glu Glu Leu Tyr Ala Ser Asp

180 185 190

His Phe Ala His Thr Ala Asn Gln His Ile Ile Ile Glu Gly Thr Gln

195 200 205

Gly Tyr Gly Leu Ser Leu Arg Ala Ser Gly Asn Tyr Pro Gln Val Thr

210 215 220

Ser Ser Asp Cys Arg Ser Ile Asp Phe Leu Ala Met Ala Gly Ile Asp

225 230 235 240

Pro Thr Arg Cys Asp Thr Gln Ile Gln Asn Trp Val Val Cys Arg Val

245 250 255

Phe Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Gly Glu Thr

260 265 270

Ser Trp Ala Glu Leu Gly Leu Glu Glu Glu Lys Thr Thr Val Thr Gln

275 280 285

Lys Val Arg Arg Val Gly Met Trp Asp Gln Asp Leu Val Ala Ala Ala

290 295 300

Val Gln Ala Asn Gly Gly His Asn Ala Asn Val Val Ile Thr Met Ile

305 310 315 320

Asp Gln Val Ile Pro Gly Phe Asp Glu Val Thr Pro Glu Ile Leu Glu

325 330 335

Lys Val Gln Ala Gly Glu Ile Thr Gly Asp Ala Val Pro Arg Ala Leu

340 345 350

Asp Glu Ala Ile Glu Trp Ile Asn Ala His Ala Ser Ala Glu Gln Ile

355 360 365

Gly Ala Pro Ile Ala Ala Phe Thr Tyr Ser Pro Thr Gln Ile Val Phe

370 375 380

Thr Gln Ala Ala Leu Arg Arg Arg Gly Glu Gln Gly Gly Gly Gly Leu

385 390 395 400

Ala Asp Ala Leu Ala Gln Ala Phe Glu Ser Ala Leu Ile Gly Glu Asp

405 410 415

Glu Asn

<210> 42

<211> 405

<212> PRT

<213> Microbacterium phage Sucha (Microbacterium phase Sucha)

<400> 42

Met Gln Tyr Val Ser Thr Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Lys Ser Ala Ala Val Asp Ala

20 25 30

Arg Thr Trp Leu Glu His Asn Pro Asp Gln Pro Leu Pro Asp Thr Ile

35 40 45

Asn Ile Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp Asp

50 55 60

Gln Gly Gln Lys Phe Ala Leu Arg Gln Val Pro Val Gly Ala Val Tyr

65 70 75 80

Glu Asp Val Gln Leu Tyr Ile Ala Pro Gly Ser Glu Ile Asp Ile Glu

85 90 95

Val Leu Tyr Ser Glu Ile Glu Ala Leu Glu Ala Ala Gly His Pro Ile

100 105 110

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

115 120 125

His Lys Glu Ala Glu Gly Ala Leu Val Gly Gly Ile Gly Ser Thr Gly

130 135 140

Lys Gly Ile Gly Ala Ala Arg Ala Ala Arg Leu Met Arg Ser Ala Gln

145 150 155 160

Thr Ile Gly Asp Tyr Phe Asp Ala Thr Gly Met Gly Thr Met Trp Glu

165 170 175

Trp Arg Glu Pro Gly Asp Trp Tyr Ala Thr Asp Asp Phe Val His Gln

180 185 190

Arg Met Ser His Leu Ile Ile Glu Gly Thr Gln Gly Tyr Gly Leu Ser

195 200 205

Leu Arg Ala Ser Gly Phe Tyr Pro Tyr Val Thr Ser Ser Asp Ala Arg

210 215 220

Ala Ile Asp Phe Gln Ala Met Ala Gly Val Asp Pro Thr Arg Cys Asn

225 230 235 240

Val Lys Ala Thr Asn Trp Val Val Ala Arg Val Tyr Pro Ile Arg Val

245 250 255

Ala Gly Asn Ser Gly Pro Met Leu Gly Glu Thr Thr Trp Asp Glu Leu

260 265 270

Gly Leu Pro Glu Glu Lys Thr Thr Val Thr Gln Lys Val Arg Arg Val

275 280 285

Gly Ala Trp Asp Val Glu Leu Leu Lys Ala Ala Ile Gln Ala Asn Gly

290 295 300

Gly His Ser Ala Arg Val Ala Ile Thr Met Leu Asp Gln Val Ile Pro

305 310 315 320

Glu Leu Ala Ser Val Asp Pro Gly Lys Ile Ala Glu Gln Gly Glu Ile

325 330 335

Asp Pro Gln Ser Asp Pro Ala Leu Ala Ala Ala Trp Gln Trp Ile Glu

340 345 350

Asp Asn Ala Ser Tyr Glu Leu Ile Gly Ala His Val Gly Ala Ile Thr

355 360 365

Tyr Gly Pro Thr Lys Ile Leu Tyr Thr Gly Tyr Gly Asp Ala Gly Ser

370 375 380

Gln Asp Ala Ser Pro Ile Asp Leu Asp Ala Ile Met Ala Gln Leu Leu

385 390 395 400

Gly Gly Gly Gln Ala

405

<210> 43

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage EstebanJulior (Arthrobacter phase EstebanJulior)

<400> 43

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Ile Thr Ala Gln Leu Val Lys Gln Ala Val Lys Met Gly

20 25 30

Arg His Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Asp Gly Val Lys Tyr Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Glu Glu Ile His Phe Ala Arg Asp Asn

85 90 95

Gly His Ile Val Gln Leu Leu Val Asp Trp Asn Ala Thr Met Ile Gln

100 105 110

His His His Lys Ala Gln Glu Ala Glu Gly Lys Met Val Glu Ser Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp

130 135 140

Arg Lys Ala Lys Arg Leu Ile Asp Phe Pro Glu Ala Cys Asn Leu Leu

145 150 155 160

Gln Glu Ile Pro Gly Val Asn Val Cys Asp Thr Val Lys Tyr Leu His

165 170 175

Gly Glu Ala Ser Arg Arg Asp Val Asn Ile Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Ile His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Glu Ala Thr Gln Val Met Ile Ala Ser Arg Val

225 230 235 240

Phe Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Glu Gly Glu Thr

245 250 255

Ser Trp Glu Glu Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Gln Trp Asp Gly Ala Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Trp Ala Val Ala Asp Asp Asp Met Glu Gly

290 295 300

Gln Leu Met Leu Met Val Thr Gly Gly Pro Lys Val Met Val Gly Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Thr Thr Phe

325 330 335

Asp Asp Cys Asp Glu Ala Thr Leu Ala Lys Val Glu Glu Trp Ile Asp

340 345 350

Lys Val Tyr Arg Glu Thr Gly Ala His Thr Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Val Leu Leu Gly Ala

370 375

<210> 44

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage DreamTeam (Arthrobacter phage DreamTeam)

<400> 44

Met Ser Asn Val Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys Ala Gly

20 25 30

Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Val Glu Glu Ile Asn Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Ile Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Gln Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Ala Ala Leu Glu Leu Leu

145 150 155 160

Asn Gln Ile Pro Gly Val Arg Val Val Asp Thr Val Thr Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Ile Asp Thr Leu Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Gly Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Glu Ala Val Gln Gly Gly Pro Ser Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Glu

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 45

<211> 367

<212> PRT

<213> Prokaryotic dsDNA virus (Prokaryotic dsDNA virus sp.)

<400> 45

Met Glu Asn Arg Glu Ile Asp Ala Ile Leu Asp Leu Gln Phe Gly Ser

1 5 10 15

Thr Gly Lys Gly Ala Val Ala Gly Phe Met Ser Arg Leu Lys Lys Tyr

20 25 30

Asp Val Ala Val Thr Ala Trp Met Pro Asn Ala Gly His Thr Tyr Ile

35 40 45

Thr Ala Asn Lys His Lys Met Val His Thr Ala Leu Ala Asn Ala Cys

50 55 60

Val Ser Pro Ser Leu Lys Trp Val Leu Ile Ala Pro Ala Ser Val Leu

65 70 75 80

Asp Val Lys Ala Leu Leu Arg Glu Ala Ser Glu Ala Val Ala Ala Gly

85 90 95

Tyr Met Lys Gln Gly Val Cys Ile Ala Val His Glu Asn Ala Thr Ile

100 105 110

Leu Lys Pro Glu Tyr Ser Gln Phe Glu Arg Asp Asn Ile Lys Ser Ile

115 120 125

Gly Ser Thr Gln Lys Gly Ser Gly Ala Ala Ile Met Ala Lys Ile Thr

130 135 140

Arg Asp Pro Gln Lys Ser Val Thr Ala Gly Gln Tyr Tyr Pro His Gly

145 150 155 160

Met Ile Gly Gly Thr Glu Cys Gly Ser Val Glu Val Arg Val Val Lys

165 170 175

His Ala Glu Tyr Lys Glu Ile Leu Arg Glu Gly Lys Thr Ile Leu Leu

180 185 190

Glu Gly Ala Gln Gly Tyr Ser Leu Gly Val His Thr Gly Phe Tyr Pro

195 200 205

Phe Thr Thr Ser Arg Glu Cys Thr Ile Ala Gln Leu Cys Ser Asp Cys

210 215 220

Leu Val Ser Pro Asp Ala Ile Thr Thr Val Phe Gly Cys Ala Arg Thr

225 230 235 240

Tyr Pro Ile Arg Val Ala Asn Arg Phe Ala Asp Gly Val Met Thr Gly

245 250 255

Trp Ser Gly Pro His Tyr Lys Asp Gln Tyr Glu Thr Thr Phe Asp Ser

260 265 270

Leu Gly Gln Glu Thr Glu Lys Thr Thr Val Thr Lys Leu Pro Arg Arg

275 280 285

Val Phe Ser Trp Ser Arg Thr Gln Val Ser Glu Ala Ile Glu Ala Asn

290 295 300

Met Pro Ser Lys Leu Lys Val Ile Leu Thr Phe Cys Asp Tyr Val Thr

305 310 315 320

Leu Gln Lys Gly Glu Asp Thr Glu Gly Met Asp His Pro Glu Ile Gln

325 330 335

Asp Met Lys Lys Asp Ile Glu Asn Ala Gly Ala Gln Leu Gly Gly Thr

340 345 350

Thr Trp Gly Pro Asn His Asp Asp Phe Gln Phe His His Gly Ser

355 360 365

<210> 46

<211> 343

<212> PRT

<213> Vibrio phage J3(Vibrio phase J3)

<400> 46

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Thr Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Glu Met Met

340

<210> 47

<211> 343

<212> PRT

<213> Vibrio phage CJY (Vibrio phase CJY)

<400> 47

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Val Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Glu Met Met

340

<210> 48

<211> 343

<212> PRT

<213> Vibrio phage H1(Vibrio phase H1)

<400> 48

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Thr Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Glu Met Met

340

<210> 49

<211> 343

<212> PRT

<213> Vibrio phage H2 SGB-2014(Vibrio phase H2 SGB-2014)

<400> 49

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Val Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Glu Met Met

340

<210> 50

<211> 343

<212> PRT

<213> Vibrio phage H3(Vibrio phase H3)

<400> 50

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Thr Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Glu Met Met

340

<210> 51

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage RcigaStruga (Arthrobacter phase RcigaStruga)

<400> 51

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Ile Thr Ala Gln Leu Val Lys Gln Ala Val Lys Ser Gly

20 25 30

Arg His Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Gln Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Ala Val Leu Val Glu Glu Ile His Leu Ala Gln Asp His

85 90 95

Gly His Val Ile Gln Leu Leu Ile Asp Glu Asn Ala Thr Leu Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ala Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Asp Arg Ile Trp

130 135 140

Arg Arg Ala Arg Arg Leu Arg Asp Ser Glu Pro Ala Leu Lys Leu Leu

145 150 155 160

Ala Asp Ile Ser Gly Val His Val Ile Asp Thr Val Lys Tyr Leu His

165 170 175

Gly Gln Ala Thr Gln Pro Asn Val Asn Ile Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Glu Ala Thr Gln Val Ile Ile Ala Cys Arg Val

225 230 235 240

Phe Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Gly Glu Thr

245 250 255

Ser Trp Glu Gln Leu Asn Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Gly Ala Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Ala Ile Asp His Asp Asp Met Glu Gly

290 295 300

Gln Leu Met Gln Leu Val Ser Gly Gly Pro Lys Val Met Val Gly Leu

305 310 315 320

Thr Met Leu Asp Gln Val Val Pro Glu Ile Glu Gly Leu Thr Thr Phe

325 330 335

Asp Asp Leu Asp Glu Pro Thr Phe Ser Lys Val Glu Glu Trp Ile Asn

340 345 350

Lys Ile Tyr Asp Glu Thr Gly Ala Gln Val Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Val Leu Leu Gly Ala

370 375

<210> 52

<211> 379

<212> PRT

<213> Arthrobacter bacteriophage lucy (Arthrobacter phase lucy)

<400> 52

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys

20 25 30

Ser Asp Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu

85 90 95

Asp His Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu

115 120 125

Ser Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Val Trp Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr

165 170 175

Leu His Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn

245 250 255

Glu Thr Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala

275 280 285

Asp Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu

290 295 300

Glu Ala Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp

340 345 350

Ile Asp Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 53

<211> 379

<212> PRT

<213> Arthrobacter bacteriophage Suppii (Arthrobacter phase Suppii)

<400> 53

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Lys Leu Ala Val Lys

20 25 30

Ala Glu Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly His Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Asp Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu

85 90 95

Asp Gln Gly His Ile Leu Asp Leu Leu Ile Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Lys Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Ile Trp Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Leu Ala

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Arg Val Val Asp Thr Val Asp Tyr

165 170 175

Leu His Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ser Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Thr Leu Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Asn

245 250 255

Glu Thr Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu His Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Glu Leu Val Ala

275 280 285

Glu Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Gly Glu Asp Asn Leu

290 295 300

Glu Ala Leu Leu Trp Glu Ala Val Gln Gly Gly Pro Ser Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Glu

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp

340 345 350

Ile Glu Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 54

<211> 379

<212> PRT

<213> Arthrobacter phage Vallejo (Arthrobacter phage Vallejo)

<400> 54

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser

20 25 30

Ala Asp Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu

85 90 95

Asp His Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Ile Trp Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Thr

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr

165 170 175

Leu His Glu Ala Leu Gln Lys Pro Asn Ala His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn

245 250 255

Glu Thr Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala

275 280 285

Asp Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu

290 295 300

Glu Ala Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp

340 345 350

Ile Asp Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Val Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 55

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Immacular (Arthrobacter phase Immacular)

<400> 55

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 56

<211> 377

<212> PRT

<213> Arthrobacter phage RAP15(Arthrobacter phage RAP15)

<400> 56

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu Tyr

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 57

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Oxynfrius (Arthrobacter phage Oxynfrius)

<400> 57

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Ile Thr Ala Gln Leu Val Lys Gln Ala Val Gln Val Gly

20 25 30

Arg His Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Val Glu Glu Ile His Leu Ala Gln Asp Asn

85 90 95

Gly His Ile Ile Gln Leu Leu Ile Asp Glu Asn Ala Thr Leu Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ser Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Asp Arg Ile Trp

130 135 140

Arg Arg Ala Arg Arg Leu Arg Asp Ser Glu Ala Ala Leu Glu Leu Leu

145 150 155 160

Arg Gln Ile Ser Gly Val His Val Ile Asp Thr Val Lys Tyr Leu His

165 170 175

Gly Gln Ala Thr Gln Pro Asn Val Asn Ile Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Glu Ala Thr Gln Val Ile Ile Ala Cys Arg Val

225 230 235 240

Phe Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Gly Glu Thr

245 250 255

Ser Trp Ala Gln Leu Asn Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Gly Glu Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Ala Ile Asp His Asp Asp Met Glu Gly

290 295 300

Gln Leu Met Gln Leu Val Ser Gly Gly Pro Lys Val Met Val Gly Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Thr Thr Phe

325 330 335

Asp Asp Leu Asp Glu Pro Thr Leu Ser Lys Val Glu Glu Trp Ile Asn

340 345 350

Lys Ile Tyr Asp Glu Thr Gly Ala Gln Val Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Val Leu Leu Gly Ala

370 375

<210> 58

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Greenhouse (Arthrobacter phase Greenhouse)

<400> 58

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Ile Thr Ala Gln Leu Val Lys Gln Ala Val Lys Val Gly

20 25 30

Arg His Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Val Glu Glu Ile His Leu Ala Gln Asp Asn

85 90 95

Gly His Ile Ile Gln Leu Leu Ile Asp Glu Asn Ala Thr Leu Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ser Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Asp Arg Ile Trp

130 135 140

Arg Arg Ala Arg Arg Leu Arg Asp Ser Glu Ala Ala Leu Glu Leu Leu

145 150 155 160

Arg Gln Ile Ser Gly Val His Val Ile Asp Thr Val Lys Tyr Leu His

165 170 175

Gly Gln Ala Thr Gln Pro Asn Val Asn Ile Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Glu Ala Thr Gln Val Ile Ile Ala Cys Arg Val

225 230 235 240

Phe Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Gly Glu Thr

245 250 255

Ser Trp Ala Gln Leu Asn Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Gly Glu Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Ala Ile Asp His Asp Asp Met Glu Gly

290 295 300

Gln Leu Met Gln Leu Val Ser Gly Gly Pro Lys Val Met Val Gly Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Thr Thr Phe

325 330 335

Asp Asp Leu Asp Glu Pro Thr Leu Ser Lys Val Glu Glu Trp Ile Asn

340 345 350

Lys Ile Tyr Asp Glu Thr Gly Ala Gln Val Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Val Leu Leu Gly Ala

370 375

<210> 59

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Joann (Arthrobacter phage Joann)

<400> 59

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Ile Thr Ala Gln Leu Val Lys Gln Ala Val Gln Val Gly

20 25 30

Arg His Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Val Glu Glu Ile His Leu Ala Gln Asp Asn

85 90 95

Gly His Ile Ile Gln Leu Leu Ile Asp Glu Asn Ala Thr Leu Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ser Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Asp Arg Ile Trp

130 135 140

Arg Arg Ala Arg Arg Leu Arg Asp Ser Glu Ala Ala Leu Glu Leu Leu

145 150 155 160

Arg Gln Ile Ser Gly Val His Val Ile Asp Thr Val Lys Tyr Leu His

165 170 175

Gly Gln Ala Thr Gln Pro Asn Val Asn Ile Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Glu Ala Thr Gln Val Ile Ile Ala Cys Arg Val

225 230 235 240

Phe Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Gly Glu Thr

245 250 255

Ser Trp Glu Gln Leu Asn Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Gly Glu Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Ala Ile Asp His Asp Asp Met Glu Gly

290 295 300

Gln Leu Met Gln Leu Val Ser Gly Gly Pro Lys Val Met Val Gly Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Thr Thr Phe

325 330 335

Asp Asp Leu Asp Glu Pro Thr Leu Ser Lys Val Glu Glu Trp Ile Asn

340 345 350

Lys Ile Tyr Asp Glu Thr Gly Ala Gln Val Thr Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Val Leu Leu Gly Ala

370 375

<210> 60

<211> 379

<212> PRT

<213> Arthrobacter phage Korra (Arthrobacter phase Korra)

<400> 60

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser

20 25 30

Ala Asp Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu

85 90 95

Asp His Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Ile Trp Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr

165 170 175

Leu His Glu Ala Leu Gln Lys Pro Asn Ala His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn

245 250 255

Glu Thr Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala

275 280 285

Asp Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu

290 295 300

Glu Ala Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp

340 345 350

Ile Asp Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Val Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 61

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Pumancara (Arthrobacter phage Pumancara)

<400> 61

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Arg Glu Ala Ala Arg His Asn

20 25 30

Arg Ser Ile Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Arg Tyr His

85 90 95

Gly His Ile Leu Gln Leu Leu Val Asp Glu Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ser Glu Gly Gln Met Val Asp Arg Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Gln Leu Leu

145 150 155 160

Thr Glu Ile Pro Gly Val Lys Val Cys Asp Thr Val Ala Tyr Leu His

165 170 175

Gly Gln Ala Thr Arg Glu Glu Val Asn Ile Ile Val Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Ala Ala Val Gln Val Met Ile Ala Cys Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Glu Gly Glu Thr

245 250 255

Thr Trp Glu Glu Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Ala Ala Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Lys Ile Asp Glu Asp Asp Ile His Gly

290 295 300

Gln Leu Gln Leu Leu Val Ser Gly Gly Pro Lys Val Thr Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Val Pro Gly Ile Glu Gly Ala Thr Asp Ile

325 330 335

Asp Lys Ile Glu Pro Glu Glu Phe Ala Lys Val Glu Glu Trp Ile Glu

340 345 350

Lys Ile Tyr Arg Glu Thr Gly Ala His Thr Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Leu Leu Ile Gly Ala

370 375

<210> 62

<211> 379

<212> PRT

<213> Arthrobacter bacteriophage Wayne (Arthrobacter phase Wayne)

<400> 62

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Lys Leu Ala Val Lys

20 25 30

Ala Glu Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly His Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Asp Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu

85 90 95

Asp Gln Gly His Ile Leu Asp Leu Leu Ile Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Ile Trp Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Leu Ala

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Arg Val Val Asp Thr Val Asp Tyr

165 170 175

Leu His Thr Ala Leu Gln Lys Pro Ser Val His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Ile Leu Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Asn

245 250 255

Glu Thr Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu His Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Glu Leu Val Ala

275 280 285

Glu Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Gly Glu Asp Asn Leu

290 295 300

Glu Ala Leu Leu Trp Glu Ala Val Gln Gly Gly Pro Ser Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Glu

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp

340 345 350

Ile Glu Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 63

<211> 379

<212> PRT

<213> Arthrobacter phage Bennie (Arthrobacter phage Bennie)

<400> 63

Met Asp Met Ser Asn Val Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Val Lys

20 25 30

Gly Glu Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly Val Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu

85 90 95

Asp Asn Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Lys Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Ile Trp Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Ala Ala Leu Glu

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Arg Val Val Asp Thr Val Glu Tyr

165 170 175

Leu His Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Ile Asp Thr Val Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn

245 250 255

Glu Thr Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala

275 280 285

Asp Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu

290 295 300

Glu Ala Leu Leu Trp Gln Ala Val Gln Gly Gly Pro Ser Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Thr

325 330 335

Ser Phe Asp Asp Cys Asp Glu Ala Thr Leu Gln Lys Val Glu Ala Trp

340 345 350

Ile Asp Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 64

<211> 379

<212> PRT

<213> Arthrobacter bacteriophage DrRobert (Arthrobacter phage DrRobert)

<400> 64

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys

20 25 30

Ser Asp Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu

85 90 95

Asp His Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Val Trp Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr

165 170 175

Leu His Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn

245 250 255

Glu Thr Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala

275 280 285

Asp Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu

290 295 300

Glu Ala Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp

340 345 350

Ile Asp Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 65

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Glenn (Arthrobacter phage Glenn)

<400> 65

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Thr Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Ala His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Val Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 66

<211> 343

<212> PRT

<213> Vibrio phage phiVC8(Vibrio phage phiVC8)

<400> 66

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Val Pro Glu Leu Thr Thr Val Thr Lys Lys Val Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Glu Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Asn Asp Val

325 330 335

Glu Leu Arg Glu Asp Val Met

340

<210> 67

<211> 343

<212> PRT

<213> Vibrio phage J2(Vibrio phase J2)

<400> 67

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Thr Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Glu Met Met

340

<210> 68

<211> 343

<212> PRT

<213> Vibrio phage QH (Vibrio phase QH)

<400> 68

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Val Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Asp Met Met

340

<210> 69

<211> 343

<212> PRT

<213> Vibrio phage VP5(Vibrio phase VP5)

<400> 69

Met Lys Asn Val Asp Leu Val Ile Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Lys Asn Gly Tyr Asp Thr

20 25 30

Val Ile Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Glu Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Lys Arg Val Met Leu Gly Ala Gly Ser Val Phe Ser Ile

65 70 75 80

Asn Arg Leu Met Glu Glu Ile Glu Met Ser Lys Asp Leu Leu His Asp

85 90 95

Lys Val Ala Ile Leu Ile His Pro Met Ala Thr Val Leu Asp Glu Glu

100 105 110

Ala His Lys Lys Ala Glu Val Gly Ile Ala Thr Ser Ile Gly Ser Thr

115 120 125

Gly Gln Gly Ser Met Ala Ala Met Val Glu Lys Leu Gln Arg Asp Pro

130 135 140

Thr Asn Asn Thr Ile Val Ala Arg Asp Val Ala Gln Tyr Asp Gly Arg

145 150 155 160

Ile Ala Gln Tyr Val Cys Thr Val Glu Glu Trp Asp Met Ala Leu Met

165 170 175

Ala Ser Glu Arg Ile Leu Ala Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Leu Asn Gln Glu Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro

195 200 205

Ala Arg Phe Leu Ala Asp Met Gly Ile Pro Leu Pro Met Leu Asn Lys

210 215 220

Val Ile Gly Thr Ala Arg Cys His Pro Ile Arg Val Gly Gly Thr Ser

225 230 235 240

Gly Gly His Tyr Pro Asp Gln Glu Glu Leu Thr Trp Glu Gln Leu Gly

245 250 255

Gln Val Pro Glu Leu Thr Thr Val Thr Lys Lys Ile Arg Arg Val Phe

260 265 270

Ser Phe Ser Phe Ile Gln Met Gln Lys Ala Met Trp Thr Cys Gln Pro

275 280 285

Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Leu Ser Pro Met Gly Trp

290 295 300

Gln Asp Ile Val His Gln Ile Glu Val Ala Ala Gln Ser Arg Tyr Cys

305 310 315 320

Asp Ala Lys Val Lys Tyr Leu Gly Phe Gly Pro Thr Phe Leu Asp Val

325 330 335

Glu Leu Arg Glu Glu Met Met

340

<210> 70

<211> 391

<212> PRT

<213> cyanobacterial phage (cyanophage)

<400> 70

Met Leu Ser Ile Pro Pro Tyr Tyr Arg Val Lys Asn Cys Asn Leu Ile

1 5 10 15

Val Asp Cys Gln Tyr Gly Ser Thr Gly Lys Gly Leu Leu Ala Gly Tyr

20 25 30

Leu Gly Ala Leu Glu Ala Pro Gln Val Leu Cys Met Ala Pro Ser Pro

35 40 45

Asn Ala Gly His Thr Leu Val Glu Glu Asp Gly Thr Ala Arg Val His

50 55 60

Lys Met Leu Pro Leu Gly Ile Thr Ser Pro Ser Leu Glu Arg Ile Tyr

65 70 75 80

Leu Gly Pro Gly Ser Val Ile Asp Met Asp Arg Leu Leu Glu Glu Tyr

85 90 95

Leu Ala Leu Pro Arg Gln Val Glu Leu Trp Val His Gln Asn Ala Ala

100 105 110

Val Val Leu Gln Glu His Arg Asp Glu Glu Ala Ala Gly Gly Leu Ala

115 120 125

Pro Gly Ser Thr Arg Ser Gly Ala Gly Ser Ala Phe Ile Ala Lys Ile

130 135 140

Arg Arg Arg Pro Gly Thr Leu Leu Phe Gly Glu Ala Val Arg Asp His

145 150 155 160

Pro Leu His Gly Val Val Arg Val Val Asp Thr Arg Thr Ala Gln Asp

165 170 175

Met Leu Phe Arg Thr Arg Ser Ile Gln Ala Glu Gly Cys Gln Gly Tyr

180 185 190

Ser Leu Ser Val His His Gly Ala Tyr Pro Tyr Cys Thr Ala Arg Asp

195 200 205

Val Thr Thr Ala Gln Leu Ile Ala Asp Cys Gly Leu Pro Tyr Asp Val

210 215 220

Ala Arg Ile Ala Arg Val Val Gly Ser Met Arg Thr Tyr Pro Ile Arg

225 230 235 240

Val Ala Asn Arg Pro Glu Ala Gly Glu Trp Ser Ala Pro Cys Tyr Pro

245 250 255

Asp Ser Val Glu Cys Gln Phe Ala Asp Leu Gly Leu Glu Gln Glu Tyr

260 265 270

Thr Thr Val Thr Lys Leu Pro Arg Arg Ile Phe Thr Phe Ser Ala Ile

275 280 285

Gln Ala His Glu Ala Ile Ala Gln Asn Gly Val Asp Glu Val Phe Leu

290 295 300

Asn Phe Ala Gln Tyr Pro Pro Ser Leu Gly Ala Leu Glu Asp Ile Leu

305 310 315 320

Asp Ala Ile Glu Ala Arg Ala Glu Val Thr Tyr Val Gly Phe Gly Pro

325 330 335

Lys Ser Pro Thr Ser Thr Thr Pro Pro Pro Gly Gln Ser Ser Lys Val

340 345 350

Cys Met Pro Ala Thr Val Ala Glu Leu Gln Ala Glu Ile Ala Ala Trp

355 360 365

Ile His Pro Leu Asn Pro Asp Arg Arg Pro Gly Ala Pro Ser Pro Ser

370 375 380

Ser Trp Arg Arg Ser Gly Ser

385 390

<210> 71

<211> 359

<212> PRT

<213> cyanobacterial phage (cyanophage)

<400> 71

Met Leu Ser Ile Pro Pro Tyr Tyr Arg Val Lys Asn Cys Asn Leu Ile

1 5 10 15

Val Asp Cys Gln Tyr Gly Ser Thr Gly Lys Gly Leu Leu Ala Gly Tyr

20 25 30

Leu Gly Ala Leu Glu Ala Pro Gln Val Leu Cys Met Ala Pro Ser Pro

35 40 45

Asn Ala Gly His Thr Leu Val Glu Glu Asp Gly Thr Ala Arg Val His

50 55 60

Lys Met Leu Pro Leu Gly Ile Thr Ser Pro Ser Leu Glu Arg Ile Tyr

65 70 75 80

Leu Gly Pro Gly Ser Val Ile Asp Met Asp Arg Leu Leu Glu Glu Tyr

85 90 95

Leu Ala Leu Pro Arg Gln Val Glu Leu Trp Val His Gln Asn Ala Ala

100 105 110

Val Val Leu Gln Glu His Arg Asp Glu Glu Ala Ala Gly Gly Leu Ala

115 120 125

Pro Gly Ser Thr Arg Ser Gly Ala Gly Ser Ala Phe Ile Ala Lys Ile

130 135 140

Arg Arg Arg Pro Gly Thr Leu Leu Phe Gly Glu Ala Val Arg Asp His

145 150 155 160

Pro Leu His Gly Val Val Arg Val Val Asp Thr Arg Thr Ala Gln Asp

165 170 175

Met Leu Phe Arg Thr Arg Ser Ile Gln Ala Glu Gly Cys Gln Gly Tyr

180 185 190

Ser Leu Ser Val His His Gly Ala Tyr Pro Tyr Cys Thr Ala Arg Asp

195 200 205

Val Thr Thr Ala Gln Leu Ile Ala Asp Cys Gly Leu Pro Tyr Asp Val

210 215 220

Ala Arg Ile Ala Arg Val Val Gly Ser Met Arg Thr Tyr Pro Ile Arg

225 230 235 240

Val Ala Asn Arg Pro Glu Ala Gly Glu Trp Ser Gly Pro Cys Tyr Pro

245 250 255

Asp Ser Val Glu Cys Gln Phe Ala Asp Leu Gly Leu Glu Gln Glu Tyr

260 265 270

Thr Thr Val Thr Lys Leu Pro Arg Arg Ile Phe Thr Phe Ser Ala Ile

275 280 285

Gln Ala His Glu Ala Ile Ala Gln Asn Gly Val Asp Glu Val Phe Leu

290 295 300

Asn Phe Ala Gln Tyr Pro Pro Ser Leu Gly Ala Leu Glu Asp Ile Leu

305 310 315 320

Asp Ala Ile Glu Ala Arg Ala Glu Val Thr Tyr Val Gly Phe Gly Pro

325 330 335

Lys Val Thr Asp Val Tyr His Thr Pro Thr Arg Ala Glu Leu Glu Gly

340 345 350

Leu Tyr Ala Arg Tyr Arg Arg

355

<210> 72

<211> 432

<212> PRT

<213> Escherichia coli (strain K12Escherichia coli strain K12)

<400> 72

Met Gly Asn Asn Val Val Val Leu Gly Thr Gln Trp Gly Asp Glu Gly

1 5 10 15

Lys Gly Lys Ile Val Asp Leu Leu Thr Glu Arg Ala Lys Tyr Val Val

20 25 30

Arg Tyr Gln Gly Gly His Asn Ala Gly His Thr Leu Val Ile Asn Gly

35 40 45

Glu Lys Thr Val Leu His Leu Ile Pro Ser Gly Ile Leu Arg Glu Asn

50 55 60

Val Thr Ser Ile Ile Gly Asn Gly Val Val Leu Ser Pro Ala Ala Leu

65 70 75 80

Met Lys Glu Met Lys Glu Leu Glu Asp Arg Gly Ile Pro Val Arg Glu

85 90 95

Arg Leu Leu Leu Ser Glu Ala Cys Pro Leu Ile Leu Asp Tyr His Val

100 105 110

Ala Leu Asp Asn Ala Arg Glu Lys Ala Arg Gly Ala Lys Ala Ile Gly

115 120 125

Thr Thr Gly Arg Gly Ile Gly Pro Ala Tyr Glu Asp Lys Val Ala Arg

130 135 140

Arg Gly Leu Arg Val Gly Asp Leu Phe Asp Lys Glu Thr Phe Ala Glu

145 150 155 160

Lys Leu Lys Glu Val Met Glu Tyr His Asn Phe Gln Leu Val Asn Tyr

165 170 175

Tyr Lys Ala Glu Ala Val Asp Tyr Gln Lys Val Leu Asp Asp Thr Met

180 185 190

Ala Val Ala Asp Ile Leu Thr Ser Met Val Val Asp Val Ser Asp Leu

195 200 205

Leu Asp Gln Ala Arg Gln Arg Gly Asp Phe Val Met Phe Glu Gly Ala

210 215 220

Gln Gly Thr Leu Leu Asp Ile Asp His Gly Thr Tyr Pro Tyr Val Thr

225 230 235 240

Ser Ser Asn Thr Thr Ala Gly Gly Val Ala Thr Gly Ser Gly Leu Gly

245 250 255

Pro Arg Tyr Val Asp Tyr Val Leu Gly Ile Leu Lys Ala Tyr Ser Thr

260 265 270

Arg Val Gly Ala Gly Pro Phe Pro Thr Glu Leu Phe Asp Glu Thr Gly

275 280 285

Glu Phe Leu Cys Lys Gln Gly Asn Glu Phe Gly Ala Thr Thr Gly Arg

290 295 300

Arg Arg Arg Thr Gly Trp Leu Asp Thr Val Ala Val Arg Arg Ala Val

305 310 315 320

Gln Leu Asn Ser Leu Ser Gly Phe Cys Leu Thr Lys Leu Asp Val Leu

325 330 335

Asp Gly Leu Lys Glu Val Lys Leu Cys Val Ala Tyr Arg Met Pro Asp

340 345 350

Gly Arg Glu Val Thr Thr Thr Pro Leu Ala Ala Asp Asp Trp Lys Gly

355 360 365

Val Glu Pro Ile Tyr Glu Thr Met Pro Gly Trp Ser Glu Ser Thr Phe

370 375 380

Gly Val Lys Asp Arg Ser Gly Leu Pro Gln Ala Ala Leu Asn Tyr Ile

385 390 395 400

Lys Arg Ile Glu Glu Leu Thr Gly Val Pro Ile Asp Ile Ile Ser Thr

405 410 415

Gly Pro Asp Arg Thr Glu Thr Met Ile Leu Arg Asp Pro Phe Asp Ala

420 425 430

<210> 73

<211> 171

<212> PRT

<213> Streptomyces phage ZP6(Alteromonas phage ZP6)

<400> 73

Met Lys Ile Asn Glu Leu Met Arg Leu Gln Asp Ile Ser Arg Trp Asn

1 5 10 15

Met Ile Asn Val Thr Arg Pro Gln Ser Val Ala Glu His Ser Phe Asn

20 25 30

Val Ser Met Leu Ala Gln Ala Val Ala Lys Lys Ala Asn Glu Asn Asn

35 40 45

Glu Glu Asn Thr Phe Asn His Gln Tyr Ile Gly Ile Val Ala Leu Glu

50 55 60

His Asp Ala Val Glu Ala Val Thr Gly Asp Ile Pro Thr Pro Ala Lys

65 70 75 80

Gln Lys Met Lys Gln Leu Gly Phe Asp Phe Asn Asp Ala Phe Lys Asp

85 90 95

Pro Asp Gly Glu Thr Pro Pro His Gly Tyr Ala Leu Val Ile Lys Val

100 105 110

Cys Asp Ile Phe Glu Ser Val Met Tyr Leu Arg Asn Phe Gly Thr Gly

115 120 125

Glu Arg Ala Tyr Val Val Leu Gln Gly Leu Glu His Asn Leu Glu Glu

130 135 140

Lys Met Thr Glu Leu Ala Arg Tyr His Ala Lys Leu His Ala Ala Ala

145 150 155 160

Glu Glu Val Phe Glu Glu Ala Glu Asp Tyr Glu

165 170

<210> 74

<211> 175

<212> PRT

<213> Bacteroides bacterium (Bacteroides bacterium)

<400> 74

Met Ile Lys Ile Gln Asp Val Leu Arg Ala Gly His Ile Lys Arg Trp

1 5 10 15

Gln Ile Val Asn Thr Thr Arg Gln Gln Thr Leu Ala Glu His Leu Phe

20 25 30

Asn Val Ala Met Ile Gly Lys Thr Ile Cys Glu Arg Cys Asp Leu Glu

35 40 45

Asp Ile Lys Glu Ile Val Met Glu Trp Ala Leu Ile His Asp Leu Pro

50 55 60

Glu Val Val Cys Gly Asp Met Pro Thr Pro Thr Lys Lys Arg Ile Leu

65 70 75 80

Asp Ala Gly Phe Asp Met Glu Tyr Ile Tyr Asp Lys Ile Asp Pro Met

85 90 95

Tyr Arg Glu Val Lys Leu Glu Ala Tyr Ala Gln Ile Met Pro Asn Tyr

100 105 110

Ile Val Lys Ala Ala Asp Leu Ile Glu Ser Ile His Phe Ile Ser Asp

115 120 125

His Gly Ile Gly Arg His Ala Arg Met Val Cys Ala Arg Leu Ile Arg

130 135 140

Lys Phe Asp Asp His Ile Gly Ser Asn Leu Tyr Asp Tyr Arg Arg Glu

145 150 155 160

Ile Arg Arg Ile Tyr Asp Asp Val Ile Asn Gly Asp Phe Tyr Glu

165 170 175

<210> 75

<211> 164

<212> PRT

<213> bacteria of the genus Arthrobacter (Chloroflexi bacterium)

<400> 75

Met Arg Tyr Thr Asp Pro Met Leu Arg Asp Met Met His Val Lys Arg

1 5 10 15

Trp Ala Ile Val Pro Thr Thr Lys Gln Gln Ser Ile Ala Glu His Gln

20 25 30

Tyr Phe Val Met Leu Tyr Thr Ile Glu Leu Cys Lys Leu Thr Gly Leu

35 40 45

Thr Pro Thr Ser Asn Leu Leu Thr Tyr Ala Ala Leu His Asp Val Asp

50 55 60

Glu Ile His Ser Gly Asp Ile Pro Ala Pro Tyr Lys His Pro Ser Ile

65 70 75 80

Glu Tyr Asp Ser Lys Tyr Thr Gln Asn Leu Lys Ser Leu Leu Thr Gly

85 90 95

Ser Glu Ile Ser Leu Val Lys Leu Ala Asp Leu Met Glu Ala Thr Met

100 105 110

Phe Leu Ile Asp Glu Ala Asn Ser Gly Asn Lys Arg Ile Lys Leu Leu

115 120 125

Leu Glu Lys Val Phe Ala Glu Thr Leu Lys Ala Ala Glu Lys Phe Gly

130 135 140

Val Val Ala Ala Val Thr Tyr Met Leu Asp Glu Ala Ser Asp Tyr Arg

145 150 155 160

Gly Arg Leu Glu

<210> 76

<211> 210

<212> PRT

<213> Geoeisella bacteria (gaiella bacteria)

<400> 76

Met Val Tyr Met Gly Ser Gln Lys Ser Arg Thr Gln Asn Ile Met Asp

1 5 10 15

Gly Gly Glu Met Asn Lys Ser Lys Leu Glu Lys Ala Leu Thr Leu Ser

20 25 30

His Val Pro Arg Trp Ala Ile Val Glu Val Ala Lys Pro Gln Thr Val

35 40 45

Ala Glu His Ser Tyr Arg Thr Ala Val Phe Ala Val Glu Leu Ala Glu

50 55 60

Arg Ile Cys Lys Ala Asn Ala Leu Ile Val Leu Asp Met Ala Trp Val

65 70 75 80

Met Ile Arg Ser Leu Phe His Asp Ala Glu Glu Ala Glu Ser Gly Asp

85 90 95

Ile Pro Thr Pro Phe Lys Gln Ala Leu Ser Gln Lys Tyr Asn Val Glu

100 105 110

Trp Asp Asn Asp Arg Asn Ala Lys Gly Asp Gly Ile Glu Gly Ala Ile

115 120 125

Val His Met Ala Asp Lys Ile Glu Ala Val Thr Tyr Leu Thr Arg Tyr

130 135 140

Gly Gln Arg Asn Asn Gly Arg Val Val Thr Phe Leu Lys Asp Glu Ile

145 150 155 160

Leu His Ala Lys Arg Leu Leu Phe Glu Val Ala Thr Lys Asn Tyr Met

165 170 175

Ser Asn Met Pro Gly Leu Asn Glu Glu Ala Ile Lys Ala Lys Ile Ser

180 185 190

Gly Asp Ile Asn Arg Ile Val Asp Asp Leu Ile Asp Ile Gly Thr Thr

195 200 205

Tyr Glu

210

<210> 77

<211> 202

<212> PRT

<213> Marine sediment genome (marine segment metagenome)

<400> 77

Met Ala Phe Glu Phe Glu Leu Arg Asp Leu Ser Tyr Val Pro Arg Trp

1 5 10 15

Ser Thr Val Arg Leu Ile Asn Pro Gln Asn Val Ala Asp His Gln Tyr

20 25 30

Phe Thr Ala Ile Tyr Ala Leu Gln Ile Cys Asp Leu Leu Asp Asp Gly

35 40 45

Ser Glu Ile Asp Ser Val Ile Ser Trp Glu Val Arg Phe His Thr Val

50 55 60

Ala Leu Ala Leu Val His Asp Leu Glu Glu Thr Phe Leu Gly Asp Ile

65 70 75 80

Pro Gly Pro Ala Lys Arg Ala Ile Val Asp Arg Asp Lys Leu Asp Glu

85 90 95

Leu Ser Tyr Gln Glu Ile Val Ala Arg Tyr Pro Ser Leu Val Asp Tyr

100 105 110

Thr Ala Pro Ile Gly Val Pro Gly Tyr Pro Asp Leu Val Arg Gly Ile

115 120 125

Ile Lys Ala Ala Ser Leu Met Asp Glu Leu Met Leu Leu Ile Gln Glu

130 135 140

Trp Arg Met Gly Asn Asn Leu Leu Lys His Val Gln Arg Asn Ser Met

145 150 155 160

Asn Arg Leu Glu Ala Val Trp Arg Ala Ile Pro Trp Asp Lys Asp Glu

165 170 175

Leu Asn Leu Ile Trp Asn Thr Glu Ile Ile Glu Ala Ile Ala Ala Ala

180 185 190

Glu His Gly Glu Leu Arg His Leu Leu Gly

195 200

<210> 78

<211> 147

<212> PRT

<213> Mesorhizobium sp. LNHC220B00(Mesorhizobium sp. LNHC 00)

<400> 78

Met Glu Asp Ile Ala His Gly Leu Ala Leu Gln Cys Arg Tyr Ala Gly

1 5 10 15

Gln Cys Leu Asp Phe Tyr Ser Val Ala Glu His Ser Leu Leu Val Ser

20 25 30

Asp Leu Val Glu Glu Asp Pro Leu Ala Ala Leu Leu His Asp Ala Ala

35 40 45

Glu Ala Phe Leu Gly Asp Ile Thr Arg Pro Leu Lys Gln Met Leu Pro

50 55 60

Asp Tyr Arg Gln Ile Glu Thr Glu Met Gln Arg Ala Ile Ala Glu Arg

65 70 75 80

Phe Gly Ile Ser Thr Gln Ser Ser Pro Ala Ile Lys Arg Ala Asp Leu

85 90 95

Arg Val Leu Ala Ala Glu Gln Ala Gln Ile Met Pro Ala Gly Thr Asp

100 105 110

Glu Trp Ala Lys Arg Asp Arg Ile Ala Pro Ala Leu Val Lys Val Arg

115 120 125

Phe Leu Ser Pro Arg Glu Ala Lys Ser Ala Phe Leu Arg Arg Tyr Glu

130 135 140

Ala Leu Gln

145

<210> 79

<211> 203

<212> PRT

<213> Heryou bacterium TMED158(Opitutales bacterium TMED158)

<400> 79

Met Lys Met Arg Phe Asn Arg His Tyr Arg Thr Leu Gly Cys Val Pro

1 5 10 15

Arg Trp Ser Ile Met Arg Leu Asn Arg Gln Gln Ser Val Leu Glu His

20 25 30

Thr Ala Leu Val Ala Met Tyr Ala Met Asp Val Met Glu Ala Ile Lys

35 40 45

Tyr Lys Gly Asp Trp Leu Glu Val Val Asp Leu Ala Leu Lys His Asp

50 55 60

Leu Pro Glu Val Glu Ser Gly Asp Leu Pro Ser Pro Val Lys Arg Val

65 70 75 80

Ile Ser Thr Pro Gly Lys Met Gln Glu Tyr Glu Asp Asp Ile Met Lys

85 90 95

Arg Arg Phe Gly Thr Pro Thr Glu Tyr Thr Asp Ala Ala His Asp Ile

100 105 110

Val Lys Val Ala Asp Leu Leu Glu Ala Val Leu Lys Leu Ala Glu Glu

115 120 125

Tyr Ser Thr Gly Asn Arg Ser Val Phe Gly Val Leu Cys Gly Leu Thr

130 135 140

Ala Tyr Leu Asn Asp Ala Val Thr Lys Leu Glu Gly Gly Gln Phe Leu

145 150 155 160

Trp Asp Asp Ile His Arg Ala Ile Asp Asp Glu Leu Phe Gly Gln Asp

165 170 175

Gly Ile Arg Thr Pro Arg Glu Glu Glu Ser Ser Phe Phe Trp Lys Glu

180 185 190

Ala Leu Gln Arg Glu Glu Asp Ser His Thr Asp

195 200

<210> 80

<211> 195

<212> PRT

<213> bacteria of the genus Sinobacillus (Sinobacillus)

<400> 80

Met Asn Ala Ala Leu Pro Thr Pro Arg Gly Asn Leu Met Pro Asn Glu

1 5 10 15

Leu Thr Leu Glu Gln Arg Leu Arg Thr Ala His Val Lys Arg Trp Gln

20 25 30

Ile Val Arg Val Ala Arg Glu Gln Thr Val Ala Glu His Leu Tyr Leu

35 40 45

Val Arg Val Leu Thr Asn Glu Phe Thr Thr Ala Leu Asn Phe Ser Glu

50 55 60

Glu Asp Ser Val Met Ala Gln Gln Trp Ala Leu Glu His Asp Val Pro

65 70 75 80

Glu Val Val Thr Gly Asp Leu Asn Ser Pro Ile Lys Ala Ala Leu Arg

85 90 95

Glu Ala Val Pro His Asp Asp Pro Ile Arg Arg Ile Glu Leu Ser Leu

100 105 110

Ser Asp Ser Tyr Ala Gly Leu Tyr Glu Tyr Val Lys Asn Val Ala Pro

115 120 125

His Val Arg Ala Leu Val Lys Ile Ala Asp Leu Val Glu Ala Cys Trp

130 135 140

Phe Leu Ser Ile Glu Gly Met Gly Pro His Ala Ala Glu Val Gln Arg

145 150 155 160

Gly Leu Trp Arg Asp Ala Arg Ser Ala Ile Asp Ala Ala Glu Gln Glu

165 170 175

Phe Pro Gln Phe Asp Trp Asp Ala Ile Ala Arg Ile Ala Arg Arg Leu

180 185 190

Thr Gly Gly

195

<210> 81

<211> 170

<212> PRT

<213> Vibrio phage CJY (Vibrio phase CJY)

<400> 81

Met Met Gln Ile Gln Asn Ile Leu Arg Ala Gly His Val Pro Arg Trp

1 5 10 15

Gln Leu Cys Asp Thr Thr Arg Thr Gln Ser Ile Ala Glu His Met Phe

20 25 30

Asn Val Ala Met Ile Ala Arg His Met Cys Ala His Ile Gly Ile Thr

35 40 45

Gly Asp Glu Met Asn Glu Ile Val Met Gln Ala Leu Thr His Asp Met

50 55 60

Asp Glu Val Ile Leu Gly Asp Met Pro Thr Val Thr Lys Gln Arg Leu

65 70 75 80

Arg Glu Ala Gly Ile Glu Pro Asn Gly Leu Ile Asp Cys Thr Glu Thr

85 90 95

Ile Ile Glu Asp Pro Leu Ala Lys Gln Leu Ile Lys Ile Ala Asp Leu

100 105 110

Val Glu Ala Ala Trp Trp Ile Asp Glu His Gly Ile Gly Arg His Ala

115 120 125

Glu Arg Val Ala Glu Ile Thr Arg His Arg Leu Phe Ser Met Leu Asn

130 135 140

Asn Ala Lys Ile Asp Lys Ile Leu Thr Ser Ala Gly Phe Asp Ala Trp

145 150 155 160

Glu Arg Ile Lys His Gly Glu Leu Leu Ile

165 170

<210> 82

<211> 170

<212> PRT

<213> Vibrio phage H1(Vibrio phase H1)

<400> 82

Met Met Gln Ile Gln Asn Ile Leu Arg Ala Gly His Val Pro Arg Trp

1 5 10 15

Gln Leu Cys Asp Thr Thr Arg Thr Gln Ser Ile Ala Glu His Met Phe

20 25 30

Asn Val Ala Met Ile Ala Arg His Met Cys Ala Cys Ile Gly Ile Thr

35 40 45

Gly Asp Glu Met Asn Glu Ile Val Met Gln Ala Leu Thr His Asp Met

50 55 60

Asp Glu Val Ile Leu Gly Asp Met Pro Thr Val Thr Lys Gln Arg Leu

65 70 75 80

Arg Glu Ala Gly Ile Glu Pro Asn Gly Leu Ile Asp Cys Thr Glu Thr

85 90 95

Ile Ile Glu Asp Pro Leu Thr Lys Gln Leu Ile Lys Ile Ala Asp Leu

100 105 110

Val Glu Ala Ala Trp Trp Ile Asp Glu His Gly Ile Gly Arg His Ala

115 120 125

Glu Arg Val Ala Glu Ile Thr Arg His Arg Leu Phe Ser Met Leu Asn

130 135 140

Asn Ala Lys Ile Asp Lys Ile Leu Thr Ser Ala Gly Phe Asp Ala Trp

145 150 155 160

Glu Arg Ile Lys His Gly Glu Leu Leu Ile

165 170

<210> 83

<211> 170

<212> PRT

<213> Vibrio phage H2(Vibrio phase H2)

<400> 83

Met Met Gln Ile Gln Asn Ile Leu Arg Ala Gly His Val Pro Arg Trp

1 5 10 15

Gln Leu Cys Asp Thr Thr Arg Thr Gln Ser Ile Ala Glu His Met Phe

20 25 30

Asn Val Ala Met Ile Ala Arg His Met Cys Ala His Ile Gly Ile Thr

35 40 45

Gly Asp Glu Met Asn Glu Ile Val Met Gln Ala Leu Thr His Asp Met

50 55 60

Asp Glu Val Ile Leu Gly Asp Met Pro Thr Val Thr Lys Gln Arg Leu

65 70 75 80

Arg Glu Ala Gly Ile Glu Pro Asn Gly Leu Ile Asp Cys Thr Glu Thr

85 90 95

Ile Ile Glu Asp Pro Leu Ala Lys Gln Leu Ile Lys Ile Ala Asp Leu

100 105 110

Val Glu Ala Ala Trp Trp Ile Asp Glu His Gly Ile Gly Arg His Ala

115 120 125

Glu Arg Val Ala Glu Ile Thr Arg His Arg Leu Phe Ser Met Leu Asn

130 135 140

Asn Ala Lys Ile Asp Lys Ile Leu Thr Ser Ala Gly Phe Asp Ala Trp

145 150 155 160

Glu Arg Ile Lys His Gly Glu Leu Leu Ile

165 170

<210> 84

<211> 170

<212> PRT

<213> Vibrio phage H3(Vibrio phase H3)

<400> 84

Met Met Gln Ile Gln Asn Ile Leu Arg Ala Gly His Val Pro Arg Trp

1 5 10 15

Gln Leu Cys Asp Thr Thr Arg Thr Gln Ser Ile Ala Glu His Met Phe

20 25 30

Asn Val Ala Met Ile Ala Arg His Met Cys Ala Cys Ile Gly Ile Thr

35 40 45

Gly Asp Glu Met Asn Glu Ile Val Met Gln Ala Leu Thr His Asp Met

50 55 60

Asp Glu Val Ile Leu Gly Asp Met Pro Thr Val Thr Lys Gln Arg Leu

65 70 75 80

Arg Glu Ala Gly Ile Glu Pro Asn Gly Leu Ile Asp Cys Thr Glu Thr

85 90 95

Ile Ile Glu Asp Pro Leu Thr Lys Gln Leu Ile Lys Ile Ala Asp Leu

100 105 110

Val Glu Ala Ala Trp Trp Ile Asp Glu His Gly Ile Gly Arg His Ala

115 120 125

Glu Arg Val Ala Glu Ile Thr Arg His Arg Leu Phe Ser Met Leu Asn

130 135 140

Asn Ala Lys Ile Asp Lys Ile Leu Thr Ser Ala Gly Phe Asp Ala Trp

145 150 155 160

Glu Arg Ile Lys His Gly Glu Leu Leu Ile

165 170

<210> 85

<211> 170

<212> PRT

<213> Vibrio phage J2(Vibrio phase J2)

<400> 85

Met Met Gln Ile Gln Asn Ile Leu Arg Ala Gly His Val Pro Arg Trp

1 5 10 15

Gln Leu Cys Asp Thr Thr Arg Thr Gln Ser Ile Ala Glu His Met Phe

20 25 30

Asn Val Ala Met Ile Ala Arg His Met Cys Ala Cys Ile Gly Ile Thr

35 40 45

Gly Asp Glu Met Asn Glu Ile Val Met Gln Ala Leu Thr His Asp Met

50 55 60

Asp Glu Val Ile Leu Gly Asp Met Pro Thr Val Thr Lys Gln Arg Leu

65 70 75 80

Arg Glu Ala Gly Ile Glu Pro Asn Gly Leu Ile Asp Cys Thr Glu Thr

85 90 95

Ile Ile Glu Asp Pro Leu Thr Lys Gln Leu Ile Lys Ile Ala Asp Leu

100 105 110

Val Glu Ala Ala Trp Trp Ile Asp Glu His Gly Ile Gly Arg His Ala

115 120 125

Glu Arg Val Ala Glu Ile Thr Arg His Arg Leu Phe Ser Met Leu Asn

130 135 140

Asn Ala Lys Ile Asp Lys Ile Leu Thr Ser Ala Gly Phe Asp Ala Trp

145 150 155 160

Glu Arg Ile Lys His Gly Glu Leu Leu Ile

165 170

<210> 86

<211> 170

<212> PRT

<213> Vibrio phage J3(Vibrio phase J3)

<400> 86

Met Met Gln Ile Gln Asn Ile Leu Arg Ala Gly His Val Pro Arg Trp

1 5 10 15

Gln Leu Cys Asp Thr Thr Arg Thr Gln Ser Ile Ala Glu His Met Phe

20 25 30

Asn Val Ala Met Ile Ala Arg His Met Cys Ala Cys Ile Gly Ile Thr

35 40 45

Gly Asp Glu Met Asn Glu Ile Val Met Gln Ala Leu Thr His Asp Met

50 55 60

Asp Glu Val Ile Leu Gly Asp Met Pro Thr Val Thr Lys Gln Arg Leu

65 70 75 80

Arg Glu Ala Gly Ile Glu Pro Asn Gly Leu Ile Asp Cys Thr Glu Thr

85 90 95

Ile Ile Glu Asp Pro Leu Thr Lys Gln Leu Ile Lys Ile Ala Asp Leu

100 105 110

Val Glu Ala Ala Trp Trp Ile Asp Glu His Gly Ile Gly Arg His Ala

115 120 125

Glu Arg Val Ala Glu Ile Thr Arg His Arg Leu Phe Ser Met Leu Asn

130 135 140

Asn Ala Lys Ile Asp Lys Ile Leu Thr Ser Ala Gly Phe Asp Ala Trp

145 150 155 160

Glu Arg Ile Lys His Gly Glu Leu Leu Ile

165 170

<210> 87

<211> 170

<212> PRT

<213> Vibrio phage JSF15(Vibrio phase JSF15)

<400> 87

Met Met Gln Ile Gln Asn Ile Leu Arg Ala Gly His Val Pro Arg Trp

1 5 10 15

Gln Leu Cys Asp Thr Thr Arg Thr Gln Ser Ile Ala Glu His Met Phe

20 25 30

Asn Val Ala Met Ile Ala Arg His Met Cys Ala His Ile Gly Ile Thr

35 40 45

Gly Asp Glu Met Asn Glu Ile Val Met Gln Ala Leu Thr His Asp Met

50 55 60

Asp Glu Val Ile Leu Gly Asp Met Pro Thr Val Thr Lys Gln Arg Leu

65 70 75 80

Arg Glu Ala Gly Ile Glu Pro Asn Gly Leu Ile Asp Cys Thr Glu Thr

85 90 95

Ile Ile Glu Asp Pro Leu Ala Lys Gln Leu Ile Lys Ile Ala Asp Leu

100 105 110

Val Glu Ala Ala Trp Trp Ile Asp Glu His Gly Ile Gly Arg His Ala

115 120 125

Glu Arg Val Ala Glu Ile Thr Arg His Arg Leu Phe Ser Met Leu Asn

130 135 140

Asn Ala Lys Ile Asp Lys Ile Leu Thr Ser Ala Gly Phe Asp Ala Trp

145 150 155 160

Glu Arg Ile Lys His Gly Glu Leu Leu Ile

165 170

<210> 88

<211> 170

<212> PRT

<213> Vibrio phage JSF33(Vibrio phase JSF33)

<400> 88

Met Met Gln Ile Gln Asn Ile Leu Arg Ala Gly His Val Pro Arg Trp

1 5 10 15

Gln Leu Cys Asp Thr Thr Arg Thr Gln Ser Ile Ala Glu His Met Phe

20 25 30

Asn Val Ala Met Ile Ala Arg His Met Cys Ala His Ile Gly Ile Thr

35 40 45

Gly Asp Glu Met Asn Glu Ile Val Met Gln Ala Leu Thr His Asp Met

50 55 60

Asp Glu Val Ile Leu Gly Asp Met Pro Thr Val Thr Lys Gln Arg Leu

65 70 75 80

Arg Glu Ala Gly Ile Glu Pro Asn Gly Leu Ile Asp Cys Thr Glu Thr

85 90 95

Ile Ile Glu Asp Pro Leu Ala Lys Gln Leu Ile Lys Ile Ala Asp Leu

100 105 110

Val Glu Ala Ala Trp Trp Ile Asp Glu His Gly Ile Gly Arg His Ala

115 120 125

Glu Arg Val Ala Glu Ile Thr Arg His Arg Leu Phe Ser Met Leu Asn

130 135 140

Asn Ala Lys Ile Asp Lys Ile Leu Thr Ser Ala Gly Phe Asp Ala Trp

145 150 155 160

Glu Arg Ile Lys His Gly Glu Leu Leu Ile

165 170

<210> 89

<211> 170

<212> PRT

<213> Vibrio phage JSF9(Vibrio phase JSF9)

<400> 89

Met Met Gln Ile Gln Asn Ile Leu Arg Ala Gly His Val Pro Arg Trp

1 5 10 15

Gln Leu Cys Asp Thr Thr Arg Thr Gln Ser Ile Ala Glu His Met Phe

20 25 30

Asn Val Ala Met Ile Ala Arg His Met Cys Ala His Ile Gly Ile Thr

35 40 45

Gly Asp Glu Met Asn Glu Ile Val Met Gln Ala Leu Thr His Asp Met

50 55 60

Asp Glu Val Ile Leu Gly Asp Met Pro Thr Val Thr Lys Gln Arg Leu

65 70 75 80

Arg Glu Ala Gly Ile Glu Pro Asn Gly Leu Ile Ser Cys Thr Glu Thr

85 90 95

Ile Ile Glu Asp Pro Phe Ala Lys Gln Leu Ile Lys Ile Ala Asp Leu

100 105 110

Val Glu Ala Ala Trp Trp Ile Asp Glu His Gly Ile Gly Arg His Ala

115 120 125

Glu Arg Val Ala Glu Ile Thr Arg His Arg Leu Phe Ser Met Leu Asn

130 135 140

Asn Ala Lys Ile Asp Lys Ala Leu Thr Ser Ala Gly Phe Asp Ala Trp

145 150 155 160

Glu Arg Ile Lys His Gly Glu Leu Leu Ile

165 170

<210> 90

<211> 170

<212> PRT

<213> Vibrio phage phiVC8(Vibrio phage phiVC8)

<400> 90

Met Met Gln Ile Gln Asn Ile Leu Arg Ala Gly His Val Pro Arg Trp

1 5 10 15

Gln Leu Cys Asp Thr Thr Arg Thr Gln Ser Ile Ala Glu His Met Phe

20 25 30

Asn Val Ala Leu Ile Ala Arg His Met Cys Ala His Ile Gly Ile Asn

35 40 45

Gly Asp Glu Met Asn Glu Ile Val Val Gln Ala Leu Thr His Asp Met

50 55 60

Asp Glu Val Ile Leu Gly Asp Met Pro Thr Val Thr Lys Gln Arg Leu

65 70 75 80

Arg Glu Ala Gly Ile Glu Pro Asn Gly Leu Ile Asp Cys Val Glu Thr

85 90 95

Ile Ile Thr Asp Pro Phe Ala Lys Gln Leu Val Lys Ile Ala Asp Leu

100 105 110

Ile Glu Ala Ala Trp Trp Ile Asp Glu His Gly Ile Gly Arg His Ala

115 120 125

Glu Arg Val Ala Glu Ile Thr Arg His Arg Leu Phe Ser Met Leu Asn

130 135 140

Asn Ala Lys Val Asp Lys Ala Leu Thr Ser Ala Gly Met Asp Ala Trp

145 150 155 160

Glu Arg Ile Lys His Gly Glu Leu Leu Ile

165 170

<210> 91

<211> 192

<212> PRT

<213> Vibrio phage VP5(Vibrio phase VP5)

<400> 91

Met Ser Ile Thr Ser Phe Trp Arg Glu Cys Ile Lys Arg Leu Pro Asn

1 5 10 15

Ile Ala Gly Glu Asn Glu Met Met Gln Ile Gln Asn Ile Leu Arg Ala

20 25 30

Gly His Val Pro Arg Trp Gln Leu Cys Asp Thr Thr Arg Thr Gln Ser

35 40 45

Ile Ala Glu His Met Phe Asn Val Ala Met Ile Ala Arg His Met Cys

50 55 60

Ala His Ile Gly Ile Thr Gly Asp Glu Met Asn Glu Ile Val Met Gln

65 70 75 80

Ala Leu Thr His Asp Met Asp Glu Val Ile Leu Gly Asp Met Pro Thr

85 90 95

Val Thr Lys Gln Arg Leu Arg Glu Ala Gly Ile Glu Pro Asn Gly Leu

100 105 110

Ile Ser Cys Thr Glu Thr Ile Ile Glu Asp Pro Phe Ala Lys Gln Leu

115 120 125

Ile Lys Ile Ala Asp Leu Val Glu Ala Ala Trp Trp Ile Asp Glu His

130 135 140

Gly Ile Gly Arg His Ala Glu Arg Val Ala Glu Ile Thr Arg His Arg

145 150 155 160

Leu Phe Ser Met Leu Asn Asn Ala Lys Ile Asp Lys Ala Leu Thr Ser

165 170 175

Ala Gly Phe Asp Ala Trp Glu Arg Ile Lys His Gly Glu Leu Leu Ile

180 185 190

<210> 92

<211> 350

<212> PRT

<213> uncultured Caudovirales phage (uncultured Caudovirales phage)

<400> 92

Met Pro His Gln Ile Asp Met Ile Met Asp Phe Gln Tyr Gly Ser Thr

1 5 10 15

Gly Lys Gly Leu Ile Ala Gly Trp Leu Ala Lys Arg Glu Lys Tyr Asp

20 25 30

Thr Ala Val Cys Ala Phe Ala Thr Asn Ala Gly His Thr Tyr Thr Asp

35 40 45

Ala Glu Arg Arg Leu His Val Met Thr Gln Gln Leu Pro Thr Ser Ile

50 55 60

Thr Ser Pro Thr Val Lys Asn Ile Leu Ile Gly Pro Gly Ala Ala Ile

65 70 75 80

His Val Asp Thr Leu Leu Asp Glu Met Ile Leu Tyr Gly Glu Leu Leu

85 90 95

Lys Asp Lys Asn Ile Leu Ile His Pro Gln Ala Ala Ile Val Glu Asp

100 105 110

Tyr His Ala Glu Phe Glu Lys Ser Asp Gly Arg Thr Lys Met Gly Ser

115 120 125

Thr Ala Lys Gly Val Gly Glu Ala Tyr Ile Glu Arg Met Arg Arg Asn

130 135 140

Pro Glu Thr Asn Asn Thr Ala Lys Asn Arg Leu Lys Glu Ser Val Leu

145 150 155 160

Ile Asp Leu Ile Cys Thr Glu Arg Glu Tyr Arg Asp Val Leu Asn Lys

165 170 175

Ser Glu Ala Val Ile Val Glu Gly Ala Gln Gly Phe Ser Leu Ser Met

180 185 190

Tyr His Gly Gln Tyr Pro Tyr Val Thr Ser Arg Asp Val Thr Pro Trp

195 200 205

Gln Ile Ala Ala Asp Cys Gly Leu Pro Tyr Ser Trp Ala Ser Tyr Ile

210 215 220

Lys Val Ile Gly Thr Leu Arg Thr Phe Pro Ile Arg Val Ser Asn Arg

225 230 235 240

Asp Gly Ser Ser Gly Pro Cys Tyr Pro Asp Gln Arg Glu Ile Ala Trp

245 250 255

Gln Asp Ile Gly Arg Glu Pro Glu Leu Thr Thr Val Thr Lys Leu Pro

260 265 270

Arg Arg Ile Phe Thr Phe Ser Gln Gln Gln Leu Asp Glu Ala Leu Phe

275 280 285

His Cys Gly Gly Tyr Trp Asp Thr Arg Leu Phe Leu Asn Phe Ala Asn

290 295 300

Tyr Leu Asp Ile Gly Asp Val Glu Asp Leu Ile His Ser Ile Glu Lys

305 310 315 320

Pro His Val Leu Ser Lys Asn Pro Pro Lys Val Val Trp Val Gly Tyr

325 330 335

Gly Pro Asp Asp Asp Asp Val Asp Val Leu Val Ala Glu Arg

340 345 350

<210> 93

<211> 274

<212> PRT

<213> Gamma-Proteobacteria (Gamma bacterium)

<400> 93

Met Ser Lys Val Asp Ile Leu Val Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Ala Ile Ala Gly Tyr Leu Ala Val Thr Arg Pro Tyr Asp Thr

20 25 30

Val Val Ser Ala Asn Arg Pro Asn Ala Gly His Thr Phe Ile Asp Ala

35 40 45

Lys Gly His Lys Met Ile His Lys Val Leu Pro Asn Gly Val Val Gly

50 55 60

Ala Ser Val Arg Thr Val Leu Ile Gly Ala Gly Ala Val Phe Ser Val

65 70 75 80

Glu Gln Leu Leu Arg Glu Ile Asp Arg Leu Asp Lys Phe Gly Tyr Asn

85 90 95

Asn Phe Gly Val Tyr Ile His Glu Ala Ala Val Val Leu Thr Asp Glu

100 105 110

His Lys Ser Gly Glu Lys Glu Tyr Ser Arg Ile Gly Ser Thr Gln Gln

115 120 125

Gly Ala Ala Gln Ala Val Ile Ala Lys Met Asp Arg Asp Pro Gly Asn

130 135 140

Asp Pro Thr Ile Lys His Val Glu Ile Asn His Pro Arg Ile Ile Val

145 150 155 160

Val Ser Pro Asn Glu Tyr His Asn Lys Leu Leu Leu Ala Asn Lys Ile

165 170 175

Leu Ala Glu Gly Ala Gln Gly Tyr Ser Leu Gly Ile Asp Ala Gly Phe

180 185 190

Trp Pro Tyr Cys Thr Ser Arg Asn Cys Thr Val Asn Ser Phe Met Ser

195 200 205

Asp Met Gly Ile Pro His Thr Met Leu Asn Thr Val Ile Gly Ala Cys

210 215 220

Arg Thr Tyr Pro Ile Arg Val Ala Gly Thr Ser Gly Pro His Tyr His

225 230 235 240

Asp Gln Glu Glu Leu Asp Trp Glu Asp Val Gly Val Glu Pro Glu Lys

245 250 255

Thr Thr Val Thr Gln Arg Val Arg Arg Val Phe Thr Phe Ser Ile Gln

260 265 270

Gln Ile

<210> 94

<211> 387

<212> PRT

<213> Acinetobacter phage (Acinetobacter phase)

<400> 94

Met Lys Lys Ala Thr Val Ile Cys Asp Met Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Phe Leu Ala Glu Arg Asp Gln Pro Asp Val

20 25 30

Val Val Thr Ala Trp Ser Ala Asn Ala Gly His Thr Tyr Ile Asn Arg

35 40 45

Glu Gly Arg Lys Trp Val His Cys Met Leu Ala Asn Gly Ile Val Ser

50 55 60

Pro Lys Leu Lys Ala Val Leu Ile Gly Gly Gly Ser Gln Met Ser Ile

65 70 75 80

Pro Thr Leu Ile Ser Glu Ile Met Gly Ser Leu Asp Ile Leu Gln Gly

85 90 95

Lys Ser Ile Leu Ile His Glu Asn Ala Cys Ile Ile Gln Gln Arg His

100 105 110

Val Glu Glu Glu Ala Gly Pro Met Thr Lys Ile Gly Ser Thr Lys Lys

115 120 125

Gly Cys Gly Ala Ala Met Met Glu Lys Ile Arg Arg Asn Pro Glu Ser

130 135 140

Lys Ile Val Ala Lys Asp Phe Ile Asp Asp Gly Leu Glu Ile Pro Asp

145 150 155 160

Phe Lys Leu Asp Gly Thr Val Gly Phe Lys Asp Ile Ser Arg His Phe

165 170 175

Glu Glu Leu Gly Val Cys Ile Lys Val Val Ser Asn Glu Val Tyr Leu

180 185 190

Ser Val Leu His Lys Ala Glu Arg Val Gln Val Glu Gly Ala Gln Gly

195 200 205

Phe Ser Leu Gly Leu His Asn Gly Phe Tyr Pro Tyr Val Thr Ser Arg

210 215 220

Glu Cys Thr Pro Ala Gln Ile Cys Ser Asp Cys Asn Val Pro Ile Ser

225 230 235 240

Met Val Asp Lys Val Val Gly Thr Met Arg Thr Tyr Pro Ile Arg Val

245 250 255

Ala Asn Arg Tyr Asp Glu Asp Gly Lys Met Val Gly Trp Ser Gly Pro

260 265 270

Cys Tyr Ser Asp Gln Thr Glu Leu Thr Trp Glu Gln Met Gly Val Thr

275 280 285

Pro Glu Lys Thr Thr Val Thr Lys Leu Thr Arg Arg Ile Phe Ser Phe

290 295 300

Ser Arg Met Gln Thr Arg Gln Ala Met Gln Val Cys Met Pro Asp Glu

305 310 315 320

Ile Phe Leu Asn Phe Ala Asn Tyr Cys Ala Ser Glu Asp Glu Leu Thr

325 330 335

Ser Ile Ile Glu Val Ile Ser Asn Glu Gly Gly Asp Val Ser Tyr Ile

340 345 350

Gly Trp Gly Asp Ser Ala Ala His Ile Glu Ser Met Leu Glu Gly Asp

355 360 365

Trp Ser Asp Asp Thr Asn Pro Leu Phe Asn Gln Tyr Asn Lys Ser Leu

370 375 380

Asn Ile Ala

385

<210> 95

<211> 342

<212> PRT

<213> short-tailed phage ctpVR23(Podoviridae sp. ctpVR23)

<400> 95

Met Pro Asn Val Thr Leu Ile Val Asp Leu Gln Phe Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Glu Arg Asp Lys Pro Asp Thr

20 25 30

Val Val Asn Ala Asn Met Pro Asn Ala Gly His Thr Tyr Ile Asn Ala

35 40 45

Ala Gly Arg Lys Trp Met His Lys Val Leu Pro Asn Gly Ile Val Ser

50 55 60

Pro Asn Leu Arg Asn Val Met Leu Gly Ala Gly Ser Ile Phe Ser Leu

65 70 75 80

Asp Arg Leu Arg Glu Glu Phe Asn Asp Ser Ser Asp Ile Phe Gly Lys

85 90 95

Glu Gly Val Arg Leu Val Ile His Gln Asp Ala Ile Val Leu His Glu

100 105 110

Ser His Ala Glu Gln Glu Arg Arg Ser Leu Ser His Ile Ser Ser Thr

115 120 125

Met Gln Gly Ser Gly Ala Ala Leu Gly Ser Lys Ile Ala Arg Asn Pro

130 135 140

Leu Asp Asp His Arg Ala Ile Glu Arg Leu Lys Gly Thr Glu Phe Glu

145 150 155 160

Asp Cys Val Val Ser Gln Ala Glu Trp Leu Leu Ile Leu Ser Gln Ser

165 170 175

Lys Arg Ile Leu Ala Glu Gly Ala Gln Gly Tyr Ser Leu Gly Leu Asn

180 185 190

Ala Gly Phe Trp Pro Tyr Cys Thr Ser Arg Asp Cys Thr Pro Ala Arg

195 200 205

Phe Leu Ala Asp Cys Gly Ile Pro Val Gly Gln Gly Trp His Leu Thr

210 215 220

Val Ile Gly Thr Ala Arg Val His Pro Ile Arg Val Gly Asn Thr Ala

225 230 235 240

Asp Gly Phe Ser Gly Asp Val Tyr Pro Asp Gln Thr Glu Thr Ser Trp

245 250 255

Glu Glu Leu Gly Val Glu Ala Glu Leu Thr Thr Val Thr Lys Arg Val

260 265 270

Arg Arg Val Phe Thr Phe Ser Glu Gln Gln Ile Ala Gln Ala Ile Ala

275 280 285

Ala Cys Asn Pro Thr Trp Val Phe Leu Asn Phe Cys Asn Tyr Asp Gln

290 295 300

Val Glu Ala Asp Arg Val Glu Glu Val Ile Asn Ser Tyr Asn Glu Phe

305 310 315 320

Gly Pro Leu Val Arg Tyr Lys Gly His Gly Pro Lys Gln Ser Asp Val

325 330 335

Val Asp Leu Glu Asn Asp

340

<210> 96

<211> 344

<212> PRT

<213> Bacteroides (bacteroides)

<400> 96

Met Ser Lys Ala Asp Met Ile Val Asp Leu Gln Tyr Gly Ser Thr Gly

1 5 10 15

Lys Gly Leu Ile Ala Gly Tyr Leu Ala Val Val Arg Lys Tyr Asp Thr

20 25 30

Val Ile Thr Ala Asn Met Pro Asn Ala Gly His Thr Phe Ile Asp Thr

35 40 45

Met Gly Asn Lys Met Val His Lys Val Leu Pro Asn Gly Val Val Ser

50 55 60

Pro Arg Cys Lys Trp Ala Leu Ile Gly Pro Gly Ala Val Phe Asp Leu

65 70 75 80

Asp Gln Leu Leu Asp Glu Leu Asn His Leu Lys Asn Ile Gly Tyr Asp

85 90 95

His Phe Lys Val Gly Ile His Pro Asn Ala Val Leu Leu Lys Thr Ala

100 105 110

His Lys Leu Ser Glu Lys Asn Asn Val Ser Ile Gly Ser Thr Met Gln

115 120 125

Gly Ser Gly Ala Ala Leu Ile Glu Lys Ile Gln Arg Asp Pro Lys Lys

130 135 140

Val Thr Ile Ile Gly Gln Phe Tyr Ala Leu Asn Ser Gly Ile Met Tyr

145 150 155 160

Asn Ser Lys Ser Leu Asn Asn Ile Val Val Leu Ser His Asp Glu Tyr

165 170 175

Arg His Ile Ile Glu Asp Ser Leu Ser Ile Leu Leu Glu Gly Ala Gln

180 185 190

Gly Phe Ser Leu Gly Ile Asn Glu Arg Phe Tyr Pro Tyr Cys Thr Ser

195 200 205

Arg Asp Cys Thr Pro Ala Arg Phe Met Ala Asp Met Gly Ile Pro Leu

210 215 220

Pro Met Leu Arg Glu Val Ile Gly Thr Ala Arg Thr Tyr Pro Ile Arg

225 230 235 240

Val Gly Asn Pro Pro Gly Gly Tyr Ser Gly Ser Cys Tyr Asn Asp Gln

245 250 255

Met Glu Ile Lys Trp Ser Asp Ile Gly Ile Glu Pro Glu Leu Thr Thr

260 265 270

Val Thr Lys Arg Glu Arg Arg Leu Phe Ser Phe Ser Phe Lys Gln Ile

275 280 285

Arg Asp Ala Met Trp Ala Met Ala Pro Asp Ser Val Phe Leu Asn Phe

290 295 300

Cys Asn Tyr Cys Lys Asn Asn Pro Thr Gln Leu Glu Leu Ile Glu Ser

305 310 315 320

Ala Phe Lys Gly Lys Ile Val Trp Lys Gly Trp Gly Pro Ser Val Asp

325 330 335

Asp Ile Lys Glu Ile Lys His Gly

340

<210> 97

<211> 359

<212> PRT

<213> Stenotrophomonas phage BUCT555 (Stenotrophoromonas phage BUCT555)

<400> 97

Met Ser Ile Thr Ala Ile Val Asp Leu Gln Phe Gly Ser Thr Gly Lys

1 5 10 15

Gly Leu Ile Ala Gly Tyr Leu Ser Glu Lys Asn Asp Tyr Asp Met Val

20 25 30

Ile Ser Ala Asn Met Pro Asn Ala Gly His Thr Tyr Val Glu Ala Asp

35 40 45

Gly Thr Lys Arg Val His Lys Val Leu Pro Ser Gly Ile Tyr Ser Lys

50 55 60

Asn Leu Lys Tyr Ile Ala Ile Gly Pro Gly Ala Val Phe Asp Pro Ser

65 70 75 80

Arg Leu Glu Leu Glu Leu Glu Gly Ile Arg Lys Ala Gly Ile Lys Ala

85 90 95

Gln Val Ile Ile His Pro Gln Ala Gly Val Leu Arg Pro Glu His Lys

100 105 110

Glu Ala Glu Gln Ser Asn Leu Ser His Ile Ser Ser Thr Met Gln Gly

115 120 125

Ser Met Ala Ala Leu Val Glu Lys Met Gly Arg Ala Arg Asp Gly Ala

130 135 140

Asn Ile Ala Lys Asn Leu Pro Ala Asp Thr Val Lys Trp Leu Asn Arg

145 150 155 160

Leu Asp Cys His Ile Val Ser Asn Met Glu Trp Asn Gly Ile Thr Trp

165 170 175

Ala Met Arg Asn Ile Leu Met Glu Gly Ser Gln Gly Tyr Ser Leu Gly

180 185 190

Leu Ser Ala Gly Phe Tyr Pro Tyr Cys Thr Ser Arg Asp Cys Thr Val

195 200 205

Trp Arg Leu Leu Ala Asp Cys Gly Val Gln Asn Phe Asp Gly Lys Leu

210 215 220

Arg Val Ile Gly Thr Ala Arg Val His Pro Ile Arg Val Gly Asn Thr

225 230 235 240

Ala Asp Gly Asn Ser Gly Pro Cys Tyr Ser Asp Gln Lys Glu Leu Thr

245 250 255

Trp Glu Asp Leu Gly Gln Thr Pro Glu Thr Thr Thr Val Thr Gly Arg

260 265 270

Val Arg Arg Val Phe Thr Phe Ser Thr Gln Gln Ile Met Asp Ala Met

275 280 285

Ile Ala Asn Arg Val Asp Glu Val Phe Leu Asn Phe Cys Asn Tyr Ala

290 295 300

Pro Ser Glu Ala Ile Arg Ile Ala Gly Asn Ile Asp Thr Ile Gly Thr

305 310 315 320

Glu Leu Tyr Lys Gln Arg Gly Tyr Pro Ala Phe Val Asp Lys Val Asn

325 330 335

Met Val Arg Tyr Met Gly Phe Gly Pro Ala Gly Arg Asp Ile Leu Glu

340 345 350

Val Gly His Asp Pro Val Trp

355

<210> 98

<211> 370

<212> PRT

<213> Blasty bacteria TMED158 (Optitales bacteria TMED158)

<400> 98

Met Glu Pro Ile Pro Leu Asp Lys Met Glu Ser Tyr Ser Ile Thr Asp

1 5 10 15

Leu Gln Phe Gly Ser Thr Gly Lys Gly Leu Leu Ala Gly Phe Gln Ala

20 25 30

Met Ile Met Lys Pro Asp Val Val Val Thr Ala Trp Met Pro Asn Ala

35 40 45

Gly His Thr Tyr Phe His Pro Asn Gly Thr Glu Met Ile His Thr Met

50 55 60

Leu Ala Asn Gly Val Val Ser Pro Lys Leu Lys Thr Val Leu Ile Ala

65 70 75 80

Pro Ala Thr Val Leu Asp Val Asp Ala Leu Leu Arg Glu Leu Asn His

85 90 95

Ala Val Arg Asn Arg Thr Cys Lys Asp Asn Ile Glu Val Leu Val His

100 105 110

Glu Asn Ala Thr Val Leu Gln Pro Arg His Ser Glu Phe Glu Arg Asn

115 120 125

Glu Ile Thr Arg Ile Gly Ser Thr Gln Lys Gly Ser Gly Ala Ala Ile

130 135 140

Met Glu Arg Leu Arg Arg Asp Pro Ala Val Pro Val Thr Ala Gly Arg

145 150 155 160

Leu Tyr Pro His Gly Tyr Ile Ser Gly Ile Val Gly Thr Asp Val Glu

165 170 175

Val Arg Val Cys Asp His Ala Glu Tyr Met Asp Lys Leu Tyr Gly Ala

180 185 190

Glu Leu Leu Ala Leu Glu Gly Ala Gln Gly Tyr Ser Leu Gly Val His

195 200 205

Ser Gly Phe Tyr Pro Tyr Thr Thr Ser Arg Glu Cys Thr Val Ala Gln

210 215 220

Leu Ala Ser Asp Thr Leu Phe Asp Pro Ala Met Ile Gln His Lys Tyr

225 230 235 240

Gly Ala Cys Arg Thr Tyr Pro Ile Arg Val Ala Asn Arg Thr Lys Asp

245 250 255

Gly Ala Thr Tyr Ser Gly Trp Ser Gly Pro Cys Tyr Pro Asp Gln Glu

260 265 270

Glu Thr Thr Phe Glu Ala Ile Gly Gln Lys Thr Glu Phe Thr Thr Val

275 280 285

Thr Lys Leu Pro Arg Arg Ile Phe Thr Trp Ser Asp Arg Gln Ile Gln

290 295 300

Glu Ala Val Lys Val Asn Gly Thr Thr Gly Ile Phe Leu Asn Phe Cys

305 310 315 320

Asn Tyr Leu Gln Glu Asp Gly Asp Thr Gly Pro Ala Trp Glu Leu Val

325 330 335

Glu Arg Ile Glu Ala Leu Thr Gly Val Pro Val Val Trp Thr Gly Trp

340 345 350

Gly Pro Leu His Ser Asp Val Lys Met Thr Met His His Ala Arg Thr

355 360 365

Lys Lys

370

<210> 99

<211> 366

<212> PRT

<213> Gaiella bacteria (Gaiella bacterium)

<400> 99

Met Gln Gln Lys Arg Cys Trp Met Ile Ile Asp Gly Gln Trp Gly Ser

1 5 10 15

Thr Gly Lys Gly Leu Ile Ala Gly Tyr Leu Ala Arg Lys Phe Lys Pro

20 25 30

Gln Gly Ala Val Cys Asn Phe Gly Pro Asn Ala Gly His Thr Phe Arg

35 40 45

Tyr Glu Gly Arg Thr Val Met Thr Arg Gln Leu Pro Thr Ala Ile Val

50 55 60

Ser Pro Asp Val Lys Val Ile Leu Ile Gly Pro Gly Ala Ile Ile Asp

65 70 75 80

Pro Glu Val Leu Asp Lys Glu Met Val Glu Phe Ala Asp Leu Leu Lys

85 90 95

Asp Lys Asn Val Phe Ile His Glu Arg Ala Ala Val Thr Thr Arg Phe

100 105 110

His Arg Glu Leu Glu Gln Glu Ala Leu Ala His Ile Ser Ser Thr Gly

115 120 125

Lys Gly Thr Gly Ala Ala Met Cys Gln Lys Ile Met Arg Gly Ala Glu

130 135 140

Ser Asn Ile Ala Arg Asp Tyr Lys Asp Lys Gly Tyr Lys Trp Ser Asp

145 150 155 160

Arg Val Cys Gly His Asp Met Phe Met Ser Val Leu Leu Ser Leu Asp

165 170 175

Thr Met Gln Ile Glu Ser Ala Gln Gly Phe Glu Leu Gly Ile Asn Ser

180 185 190

Gly Ser His Tyr Pro Tyr Cys Thr Gly Arg Asp Val Thr Pro Ala Gln

195 200 205

Val Met Ala Asp Cys Ser Ile Pro His Val Tyr Phe Asn Phe Leu Thr

210 215 220

Thr Phe Cys Ser Leu Arg Thr Phe Pro Ile Arg Val Gly Asp Gln Tyr

225 230 235 240

Asp Ala Glu Gly Lys Lys Val Gly Thr Ser Gly Pro Val Tyr Gln Asp

245 250 255

Gln Glu Glu Ile Thr Phe Glu Lys Leu Gly Val Pro Asp Glu Arg Thr

260 265 270

Thr Val Thr Gly Lys Ile Arg Arg Ile Phe Thr Phe Ser Asn Tyr Gly

275 280 285

Thr Arg Arg Met Phe Gln Ser Val Arg Pro Gly Tyr Ile Phe Leu Asn

290 295 300

Phe Val Asn Tyr Leu Thr Lys Ser Pro Gly Phe Phe Asp Pro Ala Val

305 310 315 320

Ser Ala Phe Ile Met Asn Leu His Lys Gln Tyr Met Leu Ala Thr Gly

325 330 335

Val Arg Pro Asn Gln Asp Phe Val Arg Tyr Ile Gly Cys Gly Pro Asp

340 345 350

Glu Lys Asp Val Leu Asp Ala Met Asp Val Arg Leu Lys Ile

355 360 365

<210> 100

<211> 357

<212> PRT

<213> uncultured tailed phage (uncultured Caudovirales phase)

<400> 100

Met Ala His Thr Ile Asp Met Val Met Asp Phe Gln Tyr Gly Ser Thr

1 5 10 15

Gly Lys Gly Leu Ile Ala Gly Tyr Leu Ala Lys Arg Gly Asp Tyr Asp

20 25 30

Thr Ser Val Cys Ser Phe Ala Val Asn Ala Gly His Thr Tyr Ile Asp

35 40 45

Glu Ser Arg Gly Ile His Val Met Thr Gln Gln Ile Pro Thr Gly Ala

50 55 60

Leu Ser Ser Pro Thr Val Arg Gln Val Leu Ile Gly Pro Gly Ser Leu

65 70 75 80

Ile His Ala Pro Thr Leu Leu Asp Glu Ile Lys Lys Tyr Gly His Leu

85 90 95

Leu Lys Asp Lys Lys Ile Met Ile His Pro Ser Ala Ala Val Ile Glu

100 105 110

Glu Tyr His Thr Glu Gln Glu Ile Glu Trp Gly Met Ala Asn Ile Gly

115 120 125

Ser Thr Val His Gly Val Gly Ala Ala Ala Ile Glu Arg Ile Lys Arg

130 135 140

Asn Pro Val Asn Ser Asn Ile Ala Gly Ile Arg Trp Val Gly Thr Glu

145 150 155 160

Leu Glu Arg Tyr Val Ala Thr Pro Glu Gln Tyr Arg Leu Ala Leu Asn

165 170 175

Arg Ala Glu Asn Ile Leu Ile Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Met Tyr His Gly Gln Tyr Pro Tyr Thr Thr Ser Arg Asp Val Thr Pro

195 200 205

Trp Gln Ile Ala Ala Asp Cys Gly Leu Pro Phe Arg Trp Ala Ser Tyr

210 215 220

Ile Lys Val Ile Gly Ser Met Arg Cys Phe Pro Ile Arg Val Asn Asn

225 230 235 240

Arg Thr Gly Ser Ser Gly Pro Cys Tyr Pro Asp Gln Glu Glu Ile Ser

245 250 255

Phe Asn Asp Leu Gly Val Glu Pro Glu Phe Thr Thr Val Thr Lys Leu

260 265 270

Lys Arg Arg Ile Phe Thr Phe Ser Gln Gln Gln Ala Met Glu Ala Ala

275 280 285

Phe His Cys Gly Gly Tyr Trp Asn Thr Arg Val Phe Leu Asn Phe Ala

290 295 300

Asn Tyr Thr Asp Gly Val Gly Glu Leu Arg Asp Ile Ile Ser Lys Val

305 310 315 320

Glu Ser Ile Ser Glu Ile Asn Gly Asn Pro Pro Asp Val Glu Trp Ile

325 330 335

Gly Phe Gly Pro Asp Asp Gly Asp Val Asp Thr Ile Gly Glu Tyr Asn

340 345 350

Ala Ser Ala Gly Ala

355

<210> 101

<211> 356

<212> PRT

<213> uncultured tailed phage (uncultured Caudovirales phase)

<400> 101

Met Thr His Lys Val Asp Met Val Met Asp Phe Gln Tyr Gly Ser Thr

1 5 10 15

Gly Lys Gly Leu Ile Ala Gly Tyr Leu Ala Lys Arg Glu Gln Tyr Asp

20 25 30

Thr Val Val Cys Ser Phe Ala Thr Asn Ala Gly His Thr Tyr Ile Asp

35 40 45

Lys Glu Arg Gly Ile His Val Met Thr Gln Gln Leu Pro Thr Gly Ala

50 55 60

Ile Ser Ser Pro Thr Val Lys Asn Ile Leu Ile Gly Pro Gly Ala Leu

65 70 75 80

Ile His Ala Gln Thr Leu Ala Asn Glu Ile Ser Gln Asn Ala Glu Ala

85 90 95

Leu Lys Gly Lys Arg Ile Leu Ile His Pro His Ala Ala Val Val Glu

100 105 110

Asp Tyr His Ala Lys Gln Glu Ile Asp Met Gly Met Thr Lys Ile Gly

115 120 125

Ser Thr Ala Lys Gly Cys Gly Ala Ala Ala Met Glu Arg Ile Gln Arg

130 135 140

Ser Pro Asp Asn Pro Asn Ile Ala Val Thr Arg Phe Phe Gly Thr Pro

145 150 155 160

Leu Phe Gln His Val Ala Thr Leu Asp Asp Tyr Arg Asp Ala Leu Asn

165 170 175

Asp Ala Glu Asn Val Leu Val Glu Gly Ala Gln Gly Phe Ser Leu Ser

180 185 190

Met Tyr His Gly Gln Tyr Pro Tyr Thr Thr Ser Arg Asp Val Thr Pro

195 200 205

Trp Gln Ile Ala Ala Asp Cys Gly Leu Pro Tyr Arg Trp Ala Ser Tyr

210 215 220

Val Gln Val Ile Gly Ala Met Arg Thr Tyr Pro Ile Arg Val Asn Asn

225 230 235 240

Arg Asp Gly Ser Ser Gly Pro Cys Tyr Arg Asp Gln Asn Glu Leu Gln

245 250 255

Trp Asp Asp Leu Arg Gly Val Gly Ile Ala Pro Glu Leu Thr Thr Val

260 265 270

Thr Lys Leu Lys Arg Arg Ile Phe Thr Phe Ser Ala Leu Gln Ala Glu

275 280 285

Glu Ala Ser Phe His Cys Gly Gly Tyr Trp Asp Thr Lys Val Phe Leu

290 295 300

Asn Phe Ala Asn Tyr Cys Ser Asp Met Glu Glu Leu Ala Arg Ile Ile

305 310 315 320

Lys Ala Ile Glu Thr Pro Thr Lys Ile Gln Met Asn Pro Ser Arg Val

325 330 335

Ala Trp Thr Gly Trp Gly Pro Asp Asp Ser Asp Val Arg Glu Tyr Ser

340 345 350

Gly Val Thr Lys

355

<210> 102

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Wawa (Arthrobacter phase Wawa)

<400> 102

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 103

<211> 388

<212> PRT

<213> Arthrobacter phage Supakaev (Arthrobacter phase Sukaev)

<400> 103

Met Lys Arg Asp Asn Gln Gln Glu Glu Asn Lys Leu Ser Asn Val Met

1 5 10 15

Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala Lys Gly His Ala Thr

20 25 30

Ala Gln Leu Val Lys Ile Ala Thr Arg Gln Gly Arg Gln Val Val Asn

35 40 45

Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp Asp Glu

50 55 60

Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val Gly Ala Val Val Glu

65 70 75 80

Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu Ile Asp Phe Pro Val

85 90 95

Leu Leu Glu Glu Ile His Ala Ala Leu Asp Glu Gly His Ile Leu Asp

100 105 110

Leu Lys Val Asp Gln Asn Ala Thr Leu Ile Glu Tyr His His Lys Met

115 120 125

Gln Glu Gln Glu Gly Lys Met Val Glu Asn Ile Gly Ser Thr Ala Lys

130 135 140

Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp Arg Lys Ala Arg Arg

145 150 155 160

Leu Gln Asp Val Pro Glu Ala Val Ala Leu Leu Arg Gln Leu Pro Gly

165 170 175

Val Ser Val Val Asp Thr Val Asp Tyr Leu His Arg Val Ala Ser Glu

180 185 190

Arg Asn Val Asn Ile Val Val Glu Gly Thr Gln Gly Tyr Gly Leu Gly

195 200 205

Val His Thr Ala Ala Tyr Pro Gln Thr Thr Ser Ser Asp Cys Arg Ala

210 215 220

Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro Trp His Ala Gly Ile

225 230 235 240

Asp Lys Val Gln Val Leu Ile Ala Cys Arg Val Tyr Pro Ile Arg Val

245 250 255

Ala Gly Asn Ser Gly Pro Met Lys Asn Glu Thr Thr Trp Glu Ala Leu

260 265 270

Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg Val

275 280 285

Gly Asp Trp Asp Gly Glu Leu Val Ala Glu Ala Phe Arg Ala Asn Gly

290 295 300

Gly Val Val Ile Pro Glu Asp Asp Val Glu Ala Leu Leu Trp Gln Gly

305 310 315 320

Val Thr Gly Gly Pro Arg Val Ala Val Ala Leu Thr Met Leu Asp Gln

325 330 335

Val Ile Pro Glu Ile Val Gly Leu Glu Ser Phe Asp Asp Cys Asp Glu

340 345 350

Val Val Leu Gln Lys Val Glu Glu Trp Ile Asn Lys Val Tyr Ala Glu

355 360 365

Thr Gly Ala Ile Val Thr Met Val Thr Thr Ser Pro Lys Thr Ala Val

370 375 380

Leu Leu Gly Val

385

<210> 104

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Rozby (Arthrobacter phage Rozby)

<400> 104

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 105

<211> 388

<212> PRT

<213> Arthrobacter bacteriophage Riovina (Arthrobacter phage Riovina)

<400> 105

Met Lys Arg Asp Asn Gln Gln Glu Glu Asn Lys Leu Ser Asn Val Met

1 5 10 15

Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala Lys Gly His Ala Thr

20 25 30

Ala Gln Leu Val Lys Ile Ala Thr Arg Gln Gly Arg Gln Val Val Asn

35 40 45

Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp Asp Glu

50 55 60

Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val Gly Ala Val Val Glu

65 70 75 80

Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu Ile Asp Phe Pro Val

85 90 95

Leu Leu Glu Glu Ile His Ala Ala Leu Asp Glu Gly His Ile Leu Asp

100 105 110

Leu Lys Val Asp Gln Asn Ala Thr Leu Ile Glu Tyr His His Lys Met

115 120 125

Gln Glu Gln Glu Gly Lys Met Val Glu Asn Ile Gly Ser Thr Ala Lys

130 135 140

Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp Arg Lys Ala Arg Arg

145 150 155 160

Leu Gln Asp Val Pro Glu Ala Val Ala Leu Leu Arg Gln Leu Pro Gly

165 170 175

Val Ser Val Val Asp Thr Val Asp Tyr Leu His Arg Val Ala Ser Glu

180 185 190

Arg Asn Val Asn Ile Val Val Glu Gly Thr Gln Gly Tyr Gly Leu Gly

195 200 205

Val His Thr Ala Ala Tyr Pro Gln Thr Thr Ser Ser Asp Cys Arg Ala

210 215 220

Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro Trp His Ala Gly Ile

225 230 235 240

Asp Lys Val Gln Val Leu Ile Ala Cys Arg Val Tyr Pro Ile Arg Val

245 250 255

Ala Gly Asn Ser Gly Pro Met Lys Asn Glu Thr Thr Trp Glu Ala Leu

260 265 270

Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg Val

275 280 285

Gly Asp Trp Asp Gly Glu Leu Val Ala Glu Ala Phe Arg Ala Asn Gly

290 295 300

Gly Val Val Ile Pro Glu Asp Asp Val Glu Ala Leu Leu Trp Gln Gly

305 310 315 320

Val Thr Gly Gly Pro Arg Val Ala Val Ala Leu Thr Met Leu Asp Gln

325 330 335

Val Ile Pro Glu Ile Ala Gly Leu Glu Ser Phe Asp Asp Cys Asp Glu

340 345 350

Val Val Leu Gln Lys Val Glu Glu Trp Ile Asn Lys Val Tyr Ala Glu

355 360 365

Thr Gly Ala Ile Val Thr Met Val Thr Thr Ser Pro Lys Thr Ala Val

370 375 380

Leu Leu Gly Val

385

<210> 106

<211> 388

<212> PRT

<213> Arthrobacter bacteriophage OMalley (Arthrobacter phage OMalley)

<400> 106

Met Lys Arg Asp Asn Gln Gln Glu Glu Asn Lys Leu Ser Asn Val Met

1 5 10 15

Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala Lys Gly His Ala Thr

20 25 30

Ala Gln Leu Val Lys Ile Ala Thr Arg Gln Gly Arg Gln Val Val Asn

35 40 45

Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp Asp Glu

50 55 60

Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val Gly Ala Val Val Glu

65 70 75 80

Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu Ile Asp Phe Pro Val

85 90 95

Leu Leu Glu Glu Ile His Ala Ala Leu Asp Glu Gly His Ile Leu Asp

100 105 110

Leu Lys Val Asp Gln Asn Ala Thr Leu Ile Glu Tyr His His Lys Met

115 120 125

Gln Glu Gln Glu Gly Lys Met Val Glu Asn Ile Gly Ser Thr Ala Lys

130 135 140

Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp Arg Lys Ala Arg Arg

145 150 155 160

Leu Gln Asp Val Pro Glu Ala Val Ala Leu Leu Arg Gln Leu Pro Gly

165 170 175

Val Ser Val Val Asp Thr Val Asp Tyr Leu His Arg Val Ala Ser Glu

180 185 190

Arg Asn Val Asn Ile Val Val Glu Gly Thr Gln Gly Tyr Gly Leu Gly

195 200 205

Val His Thr Ala Ala Tyr Pro Gln Thr Thr Ser Ser Asp Cys Arg Ala

210 215 220

Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro Trp His Ala Gly Ile

225 230 235 240

Asp Lys Val Gln Val Leu Ile Ala Cys Arg Val Tyr Pro Ile Arg Val

245 250 255

Ala Gly Asn Ser Gly Pro Met Lys Asn Glu Thr Thr Trp Glu Ala Leu

260 265 270

Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg Val

275 280 285

Gly Asp Trp Asp Gly Glu Leu Val Ala Glu Ala Phe Arg Ala Asn Gly

290 295 300

Gly Val Val Ile Pro Glu Asp Asp Val Glu Ala Leu Leu Trp Gln Gly

305 310 315 320

Val Thr Gly Gly Pro Arg Val Ala Val Ala Leu Thr Met Leu Asp Gln

325 330 335

Val Ile Pro Glu Ile Ala Gly Leu Glu Ser Phe Asp Asp Cys Asp Glu

340 345 350

Val Val Leu Gln Lys Val Glu Glu Trp Ile Asn Lys Val Tyr Ala Glu

355 360 365

Thr Gly Ala Ile Val Thr Met Val Thr Thr Ser Pro Lys Thr Ala Val

370 375 380

Leu Leu Gly Val

385

<210> 107

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Nancia (Arthrobacter phase Nancia)

<400> 107

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys Ser Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Ser Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 108

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Lasagna (Arthrobacter phage Lasagna)

<400> 108

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys Ser Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Ser Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 109

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage GreenHearts (Arthrobacter phage GreenHearts)

<400> 109

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Ile Thr Ala Gln Leu Val Lys Gln Ala Val Gln Val Gly

20 25 30

Arg His Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Val Glu Glu Ile His Leu Ala Gln Asp Asn

85 90 95

Gly His Ile Ile Gln Leu Leu Ile Asp Glu Asn Ala Thr Leu Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ser Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Asp Arg Ile Trp

130 135 140

Arg Arg Ala Arg Arg Leu Arg Asp Ser Glu Ala Ala Leu Glu Leu Leu

145 150 155 160

Arg Gln Ile Ser Gly Val His Val Ile Asp Thr Val Lys Tyr Leu His

165 170 175

Gly Gln Ala Thr Gln Pro Asn Val Asn Ile Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Glu Ala Thr Gln Val Ile Ile Ala Cys Arg Val

225 230 235 240

Phe Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Gly Glu Thr

245 250 255

Ser Trp Ala Gln Leu Asn Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Gly Glu Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Ala Ile Asp His Asp Asp Met Glu Gly

290 295 300

Gln Leu Met Gln Leu Val Ser Gly Gly Pro Lys Val Met Val Gly Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Thr Thr Phe

325 330 335

Asp Asp Leu Asp Glu Pro Thr Leu Ser Lys Val Glu Glu Trp Ile Asn

340 345 350

Lys Ile Tyr Asp Glu Thr Gly Ala Gln Val Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Val Leu Leu Gly Ala

370 375

<210> 110

<211> 388

<212> PRT

<213> Arthrobacter bacteriophage Eurotia (Arthrobacter phage Eurotia)

<400> 110

Met Lys Arg Asp Asn Gln Gln Glu Glu Asn Lys Leu Ser Asn Val Met

1 5 10 15

Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala Lys Gly His Ala Thr

20 25 30

Ala Gln Leu Val Lys Ile Ala Thr Arg Gln Gly Arg Gln Val Val Asn

35 40 45

Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp Asp Glu

50 55 60

Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val Gly Ala Val Val Glu

65 70 75 80

Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu Ile Asp Phe Pro Val

85 90 95

Leu Leu Glu Glu Ile His Ala Ala Leu Asp Glu Gly His Ile Leu Asp

100 105 110

Leu Lys Val Asp Gln Asn Ala Thr Leu Ile Glu Tyr His His Lys Met

115 120 125

Gln Glu Gln Glu Gly Lys Met Val Glu Asn Ile Gly Ser Thr Ala Lys

130 135 140

Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp Arg Lys Ala Arg Arg

145 150 155 160

Leu Gln Asp Val Pro Glu Ala Val Ala Leu Leu Arg Gln Leu Pro Gly

165 170 175

Val Ser Val Val Asp Thr Val Asp Tyr Leu His Arg Val Ala Ser Glu

180 185 190

Arg Asn Val Asn Ile Val Val Glu Gly Thr Gln Gly Tyr Gly Leu Gly

195 200 205

Val His Thr Ala Ala Tyr Pro Gln Thr Thr Ser Ser Asp Cys Arg Ala

210 215 220

Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro Trp His Ala Gly Ile

225 230 235 240

Asp Lys Val Gln Val Leu Ile Ala Cys Arg Val Tyr Pro Ile Arg Val

245 250 255

Ala Gly Asn Ser Gly Pro Met Lys Asn Glu Thr Thr Trp Glu Ala Leu

260 265 270

Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg Val

275 280 285

Gly Asp Trp Asp Gly Glu Leu Val Ala Glu Ala Phe Arg Ala Asn Gly

290 295 300

Gly Val Val Ile Pro Glu Asp Asp Val Glu Ala Leu Leu Trp Gln Gly

305 310 315 320

Val Thr Gly Gly Pro Arg Val Ala Val Ala Leu Thr Met Leu Asp Gln

325 330 335

Val Ile Pro Glu Ile Ala Gly Leu Glu Ser Phe Asp Asp Cys Asp Glu

340 345 350

Val Val Leu Gln Lys Val Glu Glu Trp Ile Asn Lys Val Tyr Ala Glu

355 360 365

Thr Gly Ala Ile Val Thr Met Val Thr Thr Ser Pro Lys Thr Ala Val

370 375 380

Leu Leu Gly Val

385

<210> 111

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage CristinaYang (Arthrobacter phage CristinaYang)

<400> 111

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys Ser Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Ser Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 112

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Cholula (Arthrobacter phase Cholula)

<400> 112

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 113

<211> 363

<212> PRT

<213> Gordonia phage Ghosbes)

<400> 113

Met Ala Lys Leu Asp Val Val Val Gly Ala Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly Arg Val Thr Leu Glu Leu Val Gln Arg Arg Arg Ala Glu Gly

20 25 30

Arg Gln Val Val Ser Val Arg Val Gly Gly Pro Asn Ala Gly His Val

35 40 45

Val Trp Asp Gln Gly His Arg Phe Ala Met Arg Ser Leu Pro Val Gly

50 55 60

Phe Val Asp Pro Asp Thr Leu Leu Leu Val Ala Pro Gly Ser Glu Val

65 70 75 80

Asp Leu Glu Val Leu Arg Glu Glu Val Glu Leu Val Glu Ser His Gly

85 90 95

Tyr Ser Val Arg Asp Arg Leu Trp Leu His Pro Gln Ala Thr Tyr Leu

100 105 110

His Pro Lys Tyr Arg Lys Gln Glu Gln Glu Ser Ser Leu Gly Asp Arg

115 120 125

Val Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Ala Arg Val

130 135 140

Trp Arg Thr Ala Pro Leu Val Gly Asp Val Gly Glu Phe Gly Glu Leu

145 150 155 160

Gly Arg Val Tyr Asp Phe Leu Pro His Leu Gln Asp His Ala Ser Asp

165 170 175

Pro Asn Phe Ala Val Val Val Glu Gly Thr Gln Gly Tyr Gly Leu Gly

180 185 190

Leu His Ala Gly Tyr Tyr Pro Gln Cys Thr Ser Asn Asp Ala Arg Gly

195 200 205

Leu Asp Phe Val Ala Gln Leu Gly Ala Pro Leu Pro Trp Asp Leu Pro

210 215 220

Thr Arg Thr Asp Phe Leu Val His Leu Val Val Arg Pro Phe Pro Ile

225 230 235 240

Arg Val Ala Gly Asn Ser Gly Pro Leu Ala Gly Glu Thr Ser Trp Ala

245 250 255

Glu Leu Gly Val Pro Glu Glu Arg Thr Thr Val Thr Asn Lys Val Arg

260 265 270

Arg Val Gly Gln Phe Glu Pro Glu Leu Val Ala Glu Ala Val Arg Ala

275 280 285

Asn Gly Val Arg Asn Ser Val Leu His Leu Ser Phe Ala Asp Gln Leu

290 295 300

Ala Pro Tyr Leu Glu Gly Arg Thr Glu Val Ser Glu Asp Phe Trp Ser

305 310 315 320

Ser Pro Glu Ala Asp Arg Leu Gln Glu Phe Leu Tyr Asp Leu Pro Phe

325 330 335

Ser Gln Lys Leu Leu Ser Leu Gly Thr Gly Pro Gln Thr Ser Val Trp

340 345 350

Leu Asp Ser Leu Ser Thr Tyr Thr Gly Gly Ala

355 360

<210> 114

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Aledel (Arthrobacter phage Aledel)

<400> 114

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Ala Thr Ala Gln Leu Val Lys Ile Ala Thr Arg Gln Gly

20 25 30

Arg Gln Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Val Tyr Asp Asp Glu Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Val Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Phe Pro Val Leu Leu Glu Glu Ile His Ala Ala Leu Asp Glu

85 90 95

Gly His Ile Leu Asp Leu Lys Val Asp Gln Asn Ala Thr Leu Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Gln Asp Val Pro Glu Ala Val Ala Leu Leu

145 150 155 160

Arg Gln Leu Pro Gly Val Ser Val Val Asp Thr Val Asp Tyr Leu His

165 170 175

Arg Val Ala Ser Glu Arg Asn Val Asn Ile Val Val Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Ala Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Ala Gly Ile Asp Lys Val Gln Val Leu Ile Ala Cys Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Glu Leu Val Ala Glu Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Val Ile Pro Glu Asp Asp Val Glu Ala

290 295 300

Leu Leu Trp Gln Gly Val Thr Gly Gly Pro Arg Val Ala Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Glu Ser Phe

325 330 335

Asp Asp Cys Asp Glu Val Val Leu Gln Lys Val Glu Glu Trp Ile Asn

340 345 350

Lys Val Tyr Ala Glu Thr Gly Ala Ile Val Thr Met Val Thr Thr Ser

355 360 365

Pro Lys Thr Ala Val Leu Leu Gly Val

370 375

<210> 115

<211> 388

<212> PRT

<213> Arthrobacter bacteriophage HunterDiall (Arthrobacter phage HunterDiall)

<400> 115

Met Lys Arg Asp Asn Gln Gln Glu Glu Asn Lys Leu Ser Asn Val Met

1 5 10 15

Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala Lys Gly His Ala Thr

20 25 30

Ala Gln Leu Val Lys Ile Ala Thr Arg Gln Gly Arg Gln Val Val Asn

35 40 45

Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp Asp Glu

50 55 60

Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val Gly Ala Val Val Glu

65 70 75 80

Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu Ile Asp Phe Pro Val

85 90 95

Leu Leu Glu Glu Ile His Ala Ala Leu Asp Glu Gly His Ile Leu Asp

100 105 110

Leu Lys Val Asp Gln Asn Ala Thr Leu Ile Glu Tyr His His Lys Met

115 120 125

Gln Glu Gln Glu Gly Lys Met Val Glu Asn Ile Gly Ser Thr Ala Lys

130 135 140

Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp Arg Lys Ala Arg Arg

145 150 155 160

Leu Gln Asp Val Pro Glu Ala Val Ala Leu Leu Arg Gln Leu Pro Gly

165 170 175

Val Ser Val Val Asp Thr Val Asp Tyr Leu His Arg Val Ala Ser Glu

180 185 190

Arg Asn Val Asn Ile Val Val Glu Gly Thr Gln Gly Tyr Gly Leu Gly

195 200 205

Val His Thr Ala Ala Tyr Pro Gln Thr Thr Ser Ser Asp Cys Arg Ala

210 215 220

Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro Trp His Ala Gly Ile

225 230 235 240

Asp Lys Val Gln Val Leu Ile Ala Cys Arg Val Tyr Pro Ile Arg Val

245 250 255

Ala Gly Asn Ser Gly Pro Met Lys Asn Glu Thr Thr Trp Glu Ala Leu

260 265 270

Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg Val

275 280 285

Gly Asp Trp Asp Gly Glu Leu Val Ala Glu Ala Phe Arg Ala Asn Gly

290 295 300

Gly Val Val Ile Pro Glu Asp Asp Val Glu Ala Leu Leu Trp Gln Gly

305 310 315 320

Val Thr Gly Gly Pro Arg Val Ala Val Ala Leu Thr Met Leu Asp Gln

325 330 335

Val Ile Pro Glu Ile Ala Gly Leu Glu Ser Phe Asp Asp Cys Asp Glu

340 345 350

Val Val Leu Gln Lys Val Glu Glu Trp Ile Asn Lys Val Tyr Ala Glu

355 360 365

Thr Gly Ala Ile Val Thr Met Val Thr Thr Ser Pro Lys Thr Ala Val

370 375 380

Leu Leu Gly Val

385

<210> 116

<211> 406

<212> PRT

<213> Microbacterium phage Johann's bacteriophage

<400> 116

Met Gln Phe Ile Asp Thr Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Lys Ala Ala Ala Lys Asp Ala

20 25 30

Arg Asp Tyr Ala Thr Glu His Asp Val Pro Ile Pro Glu Thr Ile Asn

35 40 45

Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp Asp Gln

50 55 60

Gly Gln Lys Phe Ala Leu Arg Gln Ile Pro Val Gly Ala Val Tyr Glu

65 70 75 80

Asp Val Lys Leu Tyr Ile Ala Pro Gly Ser Glu Ile Asp Leu Asp Val

85 90 95

Leu Tyr Ser Glu Ile Glu Ala Leu Glu Ala Ala Gly His Pro Ile Gln

100 105 110

His Arg Leu Trp Ile Ser Arg Gln Ala Thr Val Ile Thr Gln Glu His

115 120 125

Lys Asp Ala Glu Ala Ala Leu Val Gly Lys Ile Gly Ser Thr Gly Lys

130 135 140

Gly Ile Gly Ala Ala Arg Ala Ala Arg Leu Leu Arg Ser Ala Gln Thr

145 150 155 160

Ile Gly Asp Tyr Met Glu Asp Ala Gly Leu Gly Thr Met Trp Glu Trp

165 170 175

Arg Glu Pro Ser Glu Trp Tyr Ala Ser Asp Asp Phe Val His Asp Asn

180 185 190

Leu Ser His Val Leu Ile Glu Gly Thr Gln Gly Tyr Gly Leu Ser Leu

195 200 205

Arg Ala Ser Gly Asn Tyr Pro Tyr Val Thr Ser Ser Asp Ala Arg Ala

210 215 220

Ile Asp Phe Met Ala Met Ala Gly Val Asp Pro Thr Arg Cys Ser Val

225 230 235 240

Lys Ala Thr Asn Trp Val Val Ala Arg Val Phe Pro Ile Arg Val Ala

245 250 255

Gly Asn Ser Gly His Met Lys Gly Glu Thr Ser Trp Asp Glu Leu Gly

260 265 270

Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg Val Gly

275 280 285

Glu Phe Asp Val Asp Leu Leu Arg Glu Ala Val Gln Ala Asn Gly Gly

290 295 300

His Asn Ala Gln Val Val Ile Thr Met Leu Asp Gln Val Ile Pro Gly

305 310 315 320

Leu Ala Asp Val Asp Pro Asp Gln Ile His Asp Asp Glu Gly Thr Val

325 330 335

Asp Pro Ser Gln Ser Glu Tyr Leu Gln Glu Ala Leu Glu Trp Val Asn

340 345 350

Glu His Ala Gly Tyr Asp Lys Ile Gly Ala His Val Gly Ala Ile Thr

355 360 365

Phe Gly Pro Thr Lys Met Leu Phe Thr Asn His Gly Ala Asn Ala Asn

370 375 380

Asn Pro Glu Gly Gly Asp Gln Ala Met Val Asp Ala Ile Met Ser Gln

385 390 395 400

Ile Phe Gly Gly Arg Glu

405

<210> 117

<211> 377

<212> PRT

<213> Arthrobacter phage preamble (Arthrobacter phase preamble)

<400> 117

Met Ser Asn Val Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Asn Ser Asp

20 25 30

Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Ile Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Ile Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu His Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Ala Ala Leu Glu Leu Leu

145 150 155 160

Asn Gly Leu Pro Gly Val Arg Val Met Asp Thr Val Thr Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Ile Asp Thr Leu Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Gly Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Glu Ala Val Gln Gly Gly Pro Ser Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Lys Pro Glu Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 118

<211> 388

<212> PRT

<213> Arthrobacter bacteriophage vulture (Arthrobacter phage vulture)

<400> 118

Met Lys Arg Asp Asn Gln Gln Glu Glu Asn Lys Leu Ser Asn Val Met

1 5 10 15

Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala Lys Gly His Ala Thr

20 25 30

Ala Gln Leu Val Lys Ile Ala Thr Arg Gln Gly Arg Gln Val Val Asn

35 40 45

Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp Asp Glu

50 55 60

Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val Gly Ala Val Val Glu

65 70 75 80

Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu Ile Asp Phe Pro Val

85 90 95

Leu Leu Glu Glu Ile His Ala Ala Leu Asp Glu Gly His Ile Leu Asp

100 105 110

Leu Lys Val Asp Gln Asn Ala Thr Leu Ile Glu Tyr His His Lys Met

115 120 125

Gln Glu Gln Glu Gly Lys Met Val Glu Asn Ile Gly Ser Thr Ala Lys

130 135 140

Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp Arg Lys Ala Arg Arg

145 150 155 160

Leu Gln Asp Val Pro Glu Ala Val Ala Leu Leu Arg Gln Leu Pro Gly

165 170 175

Val Ser Val Val Asp Thr Val Asp Tyr Leu His Arg Val Ala Ser Glu

180 185 190

Arg Asn Val Asn Ile Val Val Glu Gly Thr Gln Gly Tyr Gly Leu Gly

195 200 205

Val His Thr Ala Ala Tyr Pro Gln Thr Thr Ser Ser Asp Cys Arg Ala

210 215 220

Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro Trp His Ala Gly Ile

225 230 235 240

Asp Lys Val Gln Val Leu Ile Ala Cys Arg Val Tyr Pro Ile Arg Val

245 250 255

Ala Gly Asn Ser Gly Pro Met Lys Asn Glu Thr Thr Trp Glu Ala Leu

260 265 270

Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg Val

275 280 285

Gly Asp Trp Asp Gly Glu Leu Val Ala Glu Ala Phe Arg Ala Asn Gly

290 295 300

Gly Val Val Ile Pro Glu Asp Asp Val Glu Ala Leu Leu Trp Gln Gly

305 310 315 320

Val Thr Gly Gly Pro Arg Val Ala Val Ala Leu Thr Met Leu Asp Gln

325 330 335

Val Ile Pro Glu Ile Ala Gly Leu Glu Ser Phe Asp Asp Cys Asp Glu

340 345 350

Val Val Leu Gln Lys Val Glu Glu Trp Ile Asn Lys Val Tyr Ala Glu

355 360 365

Thr Gly Ala Ile Val Thr Met Val Thr Thr Ser Pro Lys Thr Ala Val

370 375 380

Leu Leu Gly Val

385

<210> 119

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Kittykat (Arthrobacter phage Kittykat)

<400> 119

Met Ser Asn Val Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Asn Ser Asp

20 25 30

Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Ile Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Ile Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu His Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Arg Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Leu Gly Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val Met Asp Thr Val Thr Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Leu Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Gly Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Glu Ala Val Gln Gly Gly Pro Ser Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Lys Pro Glu Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 120

<211> 340

<212> PRT

<213> Phage 66_12(Phage 66_12)

<400> 120

Met Val Val Cys Gly Gly Gln Tyr Gly Ser Glu Ala Lys Gly Ala Ile

1 5 10 15

Thr Ala His Leu Ala Lys Asp Cys Gln Glu Pro Leu Val Val Arg Val

20 25 30

Gly Gly Pro Asn Ala Gly His Thr Val Ile Asp Asp Asp Gly Arg Glu

35 40 45

Trp Lys Leu Arg His Val Pro Val Gly Phe Val Asn Pro Ala Ala Thr

50 55 60

Leu Ala Leu Ala Pro Gly Ser Glu Val Asn Pro Arg Ile Leu Trp Glu

65 70 75 80

Glu Ile Ser Ala Leu Glu Ala Ala Gly His Lys Ile Gln Gly Arg Met

85 90 95

Cys Val Asp Pro Gln Ala Thr Leu Leu Asp Asp Thr His Val Ala Ala

100 105 110

Glu Ser Ala Ser Thr Leu Asn Asp Arg Leu Gly Ser Thr Ala Lys Gly

115 120 125

Val Gly Ala Ala Arg Ala Asp Arg Thr Trp Arg Thr Ala Glu Leu Ala

130 135 140

Ser Gly Val Leu Asn Pro Val Lys Val Pro Thr Leu Ile Glu Asp Trp

145 150 155 160

Arg Thr Ala Gly Arg Asp Val Ile Ile Glu Gly Thr Gln Gly Phe Gly

165 170 175

Leu Gly Leu His Ala Gly Leu Tyr Pro Tyr Cys Thr Ser Gly Asp Cys

180 185 190

Arg Ala Ile Asp Phe Leu Ala Gln Cys Gly Val Ser Pro Trp Ala Trp

195 200 205

Asp Pro Asp Asp Leu Asp Ile Trp Val Val Phe Arg Thr Arg Pro Ile

210 215 220

Arg Val Ala Gly Asn Ser Gly Pro Leu Met Gly Glu Thr Thr Trp Gly

225 230 235 240

Gln Leu Gly Leu Pro Glu Glu Tyr Thr Thr Val Thr Lys Arg Val Arg

245 250 255

Arg Val Gly Glu Trp Asp Ser Arg Leu Ala Tyr Ala Ala Leu Ala Ala

260 265 270

Asn Gly Gly Pro Ala Val Gln Thr His Val Ala Ile Thr Met Leu Asp

275 280 285

Gln Leu Phe Pro Glu Val Gln Gly Val Thr Thr Leu Ser Asp Leu Ser

290 295 300

Gln Arg Ala Ile Asp Trp Leu Arg Glu Lys Thr Asn Glu Leu Gly Gln

305 310 315 320

Pro Val Asp Leu Ile Gly Thr Ser Pro Ser Thr Gln Val Arg Gly Val

325 330 335

Tyr Tyr Gly Gly

340

<210> 121

<211> 358

<212> PRT

<213> Gordonia phage archimedes (Gordonia phase archimedes)

<400> 121

Met Ser Ala Ile Asp Val Ile Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly Arg Val Thr Leu Glu Arg Val Gln His Trp Ala Asp Asn Gly

20 25 30

His Ala Val Ala Ser Met Arg Val Ala Gly Pro Asn Ala Gly His Val

35 40 45

Val Trp Asp Gln Gly His Arg Phe Ala Met Arg Ser Leu Pro Val Gly

50 55 60

Phe Val Asp Pro Gly Thr Asp Leu Tyr Ile Ala Ala Gly Ser Glu Val

65 70 75 80

Asp Ile Glu Val Leu Gln Gln Glu Val Asp Leu Val Glu Ser Tyr Gly

85 90 95

Tyr Glu Val Arg Asp Arg Leu Tyr Ile His Pro Gln Ala Thr Trp Leu

100 105 110

Glu Pro Val His Arg Asp Arg Glu Ala Ser Ser Thr Leu Thr Ala Lys

115 120 125

Val Gly Ser Thr Ser Lys Gly Ile Gly Ala Ala Arg Ser Asp Arg Ile

130 135 140

Trp Arg Val Ala Asn Leu Val Gly Asp Asn Pro Ala Phe Gln Glu Leu

145 150 155 160

Gly Arg Val Ser Asp Phe Thr Glu Asp Leu Arg Ser Glu Leu Val Asp

165 170 175

Gly Ser Leu Ala Leu Val Ile Glu Gly Thr Gln Gly Tyr Gly Leu Gly

180 185 190

Leu His Ala Gly His Tyr Pro Gln Cys Thr Ser Ser Asp Ala Arg Ala

195 200 205

Ile Asp Phe Leu Ala Met Ala Gly Ile Asn Pro Trp Asp Leu Ser Arg

210 215 220

Glu Asp Leu Ala Ala His Gly Phe Arg Ile His Val Val Ile Arg Pro

225 230 235 240

Phe Pro Ile Arg Val Ala Gly Asn Ser Gly Glu Leu Ser Gly Glu Thr

245 250 255

Ser Trp Asp Glu Leu Gly Leu Glu Ala Glu Arg Thr Thr Val Thr Asn

260 265 270

Lys Ile Arg Arg Val Gly Gln Phe Asp Pro Glu Leu Val Arg Arg Ala

275 280 285

Val Leu Ala Asn Gly Val Asn Asn Val Lys Ile His Leu Ser Met Ala

290 295 300

Asp Gln Leu Ile Pro Gln Leu Ala Gly Leu Glu Asp Leu Pro Glu Gly

305 310 315 320

Trp Arg Glu Ser Glu Tyr Ala Gly Arg Leu Arg Glu Phe Ile Asp Gln

325 330 335

Ile Pro Phe Asn Glu Arg Leu Val Ser Leu Gly Thr Gly Pro His Thr

340 345 350

Arg Ile Glu Leu Phe Lys

355

<210> 122

<211> 370

<212> PRT

<213> Streptomyces phage Keanu (Streptomyces phage Keanu)

<400> 122

Met Gly Lys Leu Ile Val Val Ala Gly Ala Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Val Asp Gln Leu Ser Arg Pro Glu Val Ala Gly Ala

20 25 30

Asp Val Val Val Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Val

35 40 45

Tyr Gly Gln Cys Pro Asn Asp Cys Gln Pro Asp Ala Ser His Met Ser

50 55 60

Gly Gln Glu Trp Ile Gly His Pro Trp Arg Leu Arg Ser Val Pro Val

65 70 75 80

Gly Ala Val Ser Asn Pro Asn Ala Asp Leu Val Ile Ala Ala Gly Ser

85 90 95

Glu Ile Asp Tyr Asp Val Leu Met Ser Glu Val Val Ala Leu Asp Thr

100 105 110

Ala Gly Tyr Lys Ala Ser Asp Arg Leu Val Ile Asp Asp Gln Ala Thr

115 120 125

Met Leu Glu Pro Lys His Ile Glu Ala Glu Val Lys Asp Gly Ile Gln

130 135 140

Ala Arg Leu Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ser Asp

145 150 155 160

Arg Ile Trp Arg Tyr Ala Lys Thr Trp Gly Asp His Ile Gly Ser Glu

165 170 175

Asp Thr His Asp Thr Ala Glu Phe Met Arg Asn Arg Leu Ala Gln Gly

180 185 190

Ala Thr Val Ile Ile Glu Gly Thr Gln Gly Tyr Gly Leu Gly Leu His

195 200 205

Ala Gly His Tyr Pro Gln Cys Thr Ser Ser Asp Cys Arg Ala Val Asp

210 215 220

Phe Leu Ala Met Ala Gly Leu Ser Pro Trp Met Pro Glu Val Thr Glu

225 230 235 240

Phe Gly Val Trp Leu Ala Ala Arg Val Arg Pro Ile Arg Val Ala Gly

245 250 255

Asn Ser Gly Pro Met Lys Gly Glu Thr Thr Trp Gln Asp Leu Asn Leu

260 265 270

Pro Glu Glu Phe Thr Thr Val Thr Lys Lys Val Arg Arg Val Gly Gly

275 280 285

Trp Asp Gly Asp Leu Val Arg Arg Ala Val Ile Ala Asn Gly Gly Ala

290 295 300

Pro Val Val Arg Leu Ala Leu Thr Met Val Asp Thr Val Phe Asp Glu

305 310 315 320

Ile Arg Asn Ser Glu Gly Leu Tyr Glu Asn Ile Asp Trp Asn His Glu

325 330 335

Ala Ala Pro Pro Leu Pro Gly Met Ile Glu Ala Ile Glu Arg Glu Val

340 345 350

Asn Ala Pro Ile Arg Met Ile Ala Thr Ser Pro Thr Thr Val Leu Trp

355 360 365

Arg Ser

370

<210> 123

<211> 404

<212> PRT

<213> Microbacterium phage Cicada (Microbacterium phase Cicada)

<400> 123

Met Ser Gln Tyr Val Glu Thr Val Val Gly Gly Gln Tyr Gly Ser Glu

1 5 10 15

Ala Lys Gly His Val Thr Ala Gln Leu Val Ala Ala Ala Ala Arg Asp

20 25 30

Ala Gln Glu Phe Lys Lys Ser Asn Pro Glu Leu Asp Leu Pro Glu Thr

35 40 45

Ile Asn Ile Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp

50 55 60

Glu Ala Gly Asn Lys Phe Ala Leu Arg Gln Ile Pro Val Gly Ala Ile

65 70 75 80

Thr Pro Asp Val Gln Leu Tyr Ile Ala Pro Gly Ser Glu Ile Asp Leu

85 90 95

Asp Val Leu Tyr Ala Glu Ile Glu Leu Leu Glu Ser His Gly His Glu

100 105 110

Val Gln Ser Arg Leu Phe Ile Ser Arg Gln Ala Thr Leu Ile Gln Gly

115 120 125

His His Lys Glu Gln Glu Ala Ala Leu Val Gly Arg Ile Gly Ser Thr

130 135 140

Gly Lys Gly Ile Gly Ala Ala Arg Ala Gly His Leu Leu Arg Gln Asp

145 150 155 160

Leu Thr Ile Gly Gln Trp Phe Glu Asp Glu Gly Val Gly Thr Met Trp

165 170 175

Glu Trp Arg Glu Pro Ser Glu Trp Tyr Ala Thr Asp Asp Tyr Val His

180 185 190

Ser Val Asn Ser His Leu Val Ile Glu Gly Thr Gln Gly Phe Gly Leu

195 200 205

Ser Leu Arg Ala Ser Gly His Tyr Pro Tyr Val Thr Ser Ser Asp Ala

210 215 220

Arg Ala Ile Asp Phe Gln Ala Met Ala Gly Val Asp Pro Thr Arg Cys

225 230 235 240

Ser Val Lys Ser Thr Asn Trp Val Val Ala Arg Val Phe Pro Ile Arg

245 250 255

Val Ala Gly Asn Ser Gly Pro Met Glu Gly Glu Thr Ser Trp Glu Glu

260 265 270

Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg

275 280 285

Val Gly Ser Trp Asp Pro Glu Leu Leu Lys Ala Ala Ile Gln Ala Asn

290 295 300

Gly Gly His Asn Ala Lys Val Val Ile Thr Met Leu Asp Gln Val Ile

305 310 315 320

Pro Gly Leu Ala Gly Tyr Gln Glu Thr His Asp Glu Glu Gly Thr Val

325 330 335

Asp Thr Thr Gly Pro Leu Gln Ala Ala Met Asp Trp Ile Asn Glu His

340 345 350

Ala Ser Tyr Glu Gln Ile Gly Ala His Val Gly Ala Ile Thr Tyr Gly

355 360 365

Pro Thr Asp Phe Leu Phe Thr Gly Ala Gly Val Asp Asn Gly Gly Gly

370 375 380

Asp Leu Pro Ala Gly Leu Asp Ile Glu Ala Ile Met Gly Gln Ile Phe

385 390 395 400

Gly Gly Arg Glu

<210> 124

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage KingBob (Arthrobacter phage KingBob)

<400> 124

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Arg Glu Ala Ala Arg His Asn

20 25 30

His Ser Ile Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Lys Gly His

85 90 95

Gly His Ile Leu Gln Leu Leu Val Asp Glu Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ser Glu Gly Gln Met Val Asp Arg Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Gln Leu Leu

145 150 155 160

Thr Glu Ile Ser Gly Val Lys Val Cys Asp Thr Val Ala Tyr Leu His

165 170 175

Gly Gln Ala Ser Arg Glu Glu Val Asn Ile Ile Val Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Ala Ala Val Gln Val Met Ile Ala Cys Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Glu Gly Glu Thr

245 250 255

Thr Trp Glu Glu Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Ala Ala Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Lys Ile Asp Glu Asp Asp Ile His Gly

290 295 300

Gln Leu Gln Leu Leu Val Ser Gly Gly Pro Lys Val Thr Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Val Pro Gly Ile Glu Gly Ala Thr Asp Ile

325 330 335

Asp Lys Ile Glu Pro Glu Glu Phe Ala Lys Val Glu Glu Trp Ile Glu

340 345 350

Lys Ile Tyr Arg Glu Thr Gly Ala His Thr Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Leu Leu Ile Gly Ala

370 375

<210> 125

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Herb (Arthrobacter phage Herb)

<400> 125

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Arg Glu Ala Ala Arg His Asn

20 25 30

His Ser Ile Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Lys Gly His

85 90 95

Gly His Ile Leu Gln Leu Leu Val Asp Glu Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ser Glu Gly Gln Met Val Asp Arg Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Gln Leu Leu

145 150 155 160

Thr Glu Ile Ser Gly Val Lys Val Cys Asp Thr Val Ala Tyr Leu His

165 170 175

Gly Gln Ala Ser Arg Glu Glu Val Asn Ile Ile Val Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Ala Ala Val Gln Val Met Ile Ala Cys Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Glu Gly Glu Thr

245 250 255

Thr Trp Glu Glu Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Ala Ala Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Lys Ile Asp Glu Asp Asp Ile His Gly

290 295 300

Gln Leu Gln Leu Leu Val Ser Gly Gly Pro Lys Val Thr Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Val Pro Gly Ile Glu Gly Ala Thr Asp Ile

325 330 335

Asp Lys Ile Glu Pro Glu Glu Phe Ala Lys Val Glu Glu Trp Ile Glu

340 345 350

Lys Ile Tyr Arg Glu Thr Gly Ala His Thr Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Leu Leu Ile Gly Ala

370 375

<210> 126

<211> 377

<212> PRT

<213> Arthrobacter phage Daiboju (Arthrobacter phage Daiboju)

<400> 126

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Arg Glu Ala Ala Arg His Asn

20 25 30

His Ser Ile Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Lys Gly His

85 90 95

Gly His Ile Leu Gln Leu Leu Val Asp Glu Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ser Glu Gly Gln Met Val Asp Arg Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Gln Leu Leu

145 150 155 160

Thr Glu Ile Ser Gly Val Lys Val Cys Asp Thr Val Ala Tyr Leu His

165 170 175

Gly Gln Ala Ser Arg Glu Glu Val Asn Ile Ile Val Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Ala Ala Val Gln Val Met Ile Ala Cys Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Glu Gly Glu Thr

245 250 255

Thr Trp Glu Glu Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Ala Ala Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Lys Ile Asp Glu Asp Asp Ile His Gly

290 295 300

Gln Leu Gln Leu Leu Val Ser Gly Gly Pro Lys Val Thr Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Val Pro Gly Ile Glu Gly Ala Thr Asp Ile

325 330 335

Asp Lys Ile Glu Pro Glu Glu Phe Ala Lys Val Glu Glu Trp Ile Glu

340 345 350

Lys Ile Tyr Arg Glu Thr Gly Ala His Thr Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Leu Leu Ile Gly Ala

370 375

<210> 127

<211> 376

<212> PRT

<213> Streptomyces phage Galacta (Streptomyces phage Galacta)

<400> 127

Met Ser Gly Lys Leu Leu Val Val Val Gly Gly Gln Tyr Gly Ser Glu

1 5 10 15

Ala Lys Gly His Val Ala Asp Gln Leu Ser Arg Pro Asp Val Ala Gly

20 25 30

Asp Asn Val Val Val Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Val Tyr Gly Gln Cys Pro Ser Asp Cys Arg Pro Asp Asp Ser His Met

50 55 60

Ser Gly Asp Leu Trp Ile Gly His Pro Trp Arg Leu Arg Ser Val Pro

65 70 75 80

Val Gly Ala Val Ser Asn Pro Asn Ala Asp Leu Val Ile Ala Ala Gly

85 90 95

Ser Glu Ile Asp Tyr Asp Val Leu Met Ser Glu Val Val Ala Leu Asp

100 105 110

Ala Ala Gly Tyr Arg Val Ser Ser Arg Leu Val Ile Asp Ala Gln Ala

115 120 125

Thr Met Leu Glu Pro Lys His Ile Glu Arg Glu Val Glu Asp Lys Ile

130 135 140

Gln Glu Arg Leu Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala

145 150 155 160

Asp Arg Ile Trp Arg Tyr Ala Thr Leu Trp Gly Asp Arg Phe Pro Asp

165 170 175

Lys Ala Asp Ala Gln Asn Ser Ala Glu Phe Ile Arg Ala Arg Leu Ala

180 185 190

Gln Gly Ala Thr Val Val Ile Glu Gly Thr Gln Gly Tyr Gly Leu Gly

195 200 205

Leu His Ala Gly His Tyr Pro Gln Cys Thr Ser Ser Asp Cys Arg Ala

210 215 220

Ile Asp Phe Leu Ala Met Ala Gly Val Ser Pro Trp Trp Pro Glu Val

225 230 235 240

Ala Glu Phe Gly Val Trp Val Val Ala Arg Val Arg Pro Ile Arg Val

245 250 255

Ala Gly Asn Ser Gly Pro Ile Lys Gly Glu Thr Ser Trp Ser Glu Leu

260 265 270

Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Asn Lys Val Arg Arg Val

275 280 285

Gly Glu Trp Asp Gly Glu Leu Val Ala Glu Ala Val Arg Ala Asn Gly

290 295 300

Ser Ala Pro Val Val Arg Leu Ala Leu Thr Met Val Asp Thr Val Phe

305 310 315 320

Pro Glu Val Val Asn Gln Glu Gly Thr Leu Gly Gly Val Leu Asp Ala

325 330 335

Arg Arg Ile Thr Leu Asp Gln Ala Asn Ala Val Ala Lys Tyr Ile Ala

340 345 350

Glu Ile Glu Ala Glu Val Gly Ala Pro Val Arg Met Val Ala Thr Ser

355 360 365

Pro Thr Thr Val Leu Trp Arg Pro

370 375

<210> 128

<211> 406

<212> PRT

<213> Microbacterium bacteriophage Rasovi (Microbacterium phage Rasovi)

<400> 128

Met Gln Tyr Val Ser Thr Ile Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Lys Ala Ala Ala Lys Asp Ala

20 25 30

Arg Asp Phe Ala Thr Glu His Asp Val Pro Ile Pro Glu Thr Ile Asn

35 40 45

Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp Asp Gln

50 55 60

Gly Gln Lys Phe Ala Leu Arg Gln Ile Pro Val Gly Ala Val Tyr Glu

65 70 75 80

Asp Val Lys Leu Tyr Ile Ala Pro Gly Ser Glu Ile Asp Leu Asp Val

85 90 95

Leu Tyr Ser Glu Ile Glu Ala Leu Glu Ala Ala Gly His Pro Ile Gln

100 105 110

His Arg Leu Trp Ile Ser Arg Gln Ala Thr Val Ile Thr Gln Glu His

115 120 125

Lys Asp Ala Glu Ala Ala Leu Val Gly Asp Ile Gly Ser Thr Gly Lys

130 135 140

Gly Ile Gly Ala Ala Arg Ala Ala Arg Leu Leu Arg Ser Ala Gln Thr

145 150 155 160

Ile Gly Asp Tyr Met Glu Asp Ala Gly Leu Gly Thr Met Trp Glu Trp

165 170 175

Arg Glu Pro Ser Glu Trp Tyr Ala Ser Asp Asp Phe Val His Asp Asn

180 185 190

Leu Ser His Val Leu Ile Glu Gly Thr Gln Gly Tyr Gly Leu Ser Leu

195 200 205

Arg Ala Ser Gly Phe Tyr Pro Tyr Val Thr Ser Ser Asp Ala Arg Ala

210 215 220

Ile Asp Phe Met Ala Met Ala Gly Val Asp Pro Thr Arg Cys Ser Val

225 230 235 240

Lys Ala Thr Asn Trp Val Val Ala Arg Val Phe Pro Ile Arg Val Ala

245 250 255

Gly Asn Ser Gly Pro Met Leu Gly Glu Thr Ser Trp Asp Glu Leu Gly

260 265 270

Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg Val Gly

275 280 285

Glu Phe Asp Ala Asp Leu Leu Arg Glu Ala Val Gln Ala Asn Gly Gly

290 295 300

His Asn Ala Gln Val Val Ile Thr Met Leu Asp Gln Val Ile Pro Gly

305 310 315 320

Leu Ala Asp Val Asp Pro Asp Gln Ile His Asp Asp Glu Gly Thr Val

325 330 335

Asp Pro Ser Gln Ser Glu Tyr Leu Gln Glu Ala Leu Ala Trp Val Asn

340 345 350

Glu Asn Ala Gly Tyr Asp Lys Ile Gly Ala His Val Gly Ala Ile Thr

355 360 365

Phe Gly Pro Thr Lys Met Leu Phe Thr Asp His Gly Ala Asn Ala Asn

370 375 380

Asn Pro Glu Gly Ser Gly Gln Ala Met Val Asp Ala Ile Met Gly Gln

385 390 395 400

Leu Phe Gly Gly Gly Gln

405

<210> 129

<211> 344

<212> PRT

<213> uncultured tailed phage (uncultured Caudovirales phase)

<400> 129

Met Ala Gly Arg Leu Ile Ala Val Val Gly Gly Gln Tyr Gly Ser Glu

1 5 10 15

Gly Lys Gly Ala Val Ala Gly Phe Leu Ser Ala Asn Ser Gln Ala Ala

20 25 30

Phe Met Gly Ile Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Ile

35 40 45

Gly Lys Gly Pro Asn Gly Glu Glu Ser Tyr Pro Trp Arg Leu Arg Ser

50 55 60

Ile Pro Val Asn Ala Val Thr Ala Pro Glu Ser Asp Leu Ile Ile Ala

65 70 75 80

Ala Gly Ser Glu Ile Asp Leu Glu Val Phe Asn Arg Glu Leu Ser Glu

85 90 95

Leu Asp Gln Ala Gly Tyr Gln Ala Ser Ser Arg Ile Ile Val Asp Glu

100 105 110

Gln Ala Thr Val Leu Glu Pro Arg His His Glu Ile Glu Gln Ala Asp

115 120 125

Gly Ile Gln Ala Arg Ile Gly Ser Thr Ser Lys Gly Ile Gly Ala Ala

130 135 140

Arg Ala Asp Arg Ile Met Arg Lys Ala Ser Leu Phe Gly Gly Gly Val

145 150 155 160

Asn Thr Ser Arg Leu Val Arg Glu His Leu Gln Arg Gly Gly Thr Ala

165 170 175

Leu Ile Glu Gly Thr Gln Gly Tyr Gly Leu Gly Leu His Ala Gly Leu

180 185 190

Tyr Pro Phe Cys Thr Ser Gln Asp Cys Arg Ala Val Asp Phe Leu Ser

195 200 205

Gln Val Gly Ile Asn Pro Trp Asp Arg Ala Val Asp Leu Phe Asp Ile

210 215 220

Trp Val Thr Ala Arg Thr Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly

225 230 235 240

Pro Leu Glu Asn Glu Thr Ser Trp Glu Gln Leu Gly Leu Glu Val Glu

245 250 255

Arg Thr Thr Val Thr Gln Lys Val Arg Arg Val Gly His Phe Asp Ala

260 265 270

Lys Leu Val Arg Asp Ala Val Ile Ala Asn Gly Gly Ala Pro Thr Val

275 280 285

Ser Ile Ala Leu Thr Met Phe Asp Tyr Ile Phe Pro Glu Leu Lys Gly

290 295 300

Lys Thr Glu Val Asp Leu Ser Ala Asp Gln Arg Glu Tyr Ile His Glu

305 310 315 320

Ile Glu Asp Ala Val Gly Ala Arg Val Arg Leu Ile Gly Thr Gly Pro

325 330 335

Ser Thr Met Ala Trp Val Arg Pro

340

<210> 130

<211> 347

<212> PRT

<213> uncultured tailed phage (uncultured Caudovirales phase)

<400> 130

Met Ser Gly Lys Leu Thr Val Val Val Gly Gly Gln Tyr Gly Ser Glu

1 5 10 15

Gly Lys Gly Ala Ile Ser Gly Tyr Leu Ala Ala Gln Ala Leu Lys Glu

20 25 30

Gly Thr Pro Phe Met Gly Val Arg Val Ala Gly Pro Asn Ala Gly His

35 40 45

Thr Val Tyr Gly Val Gly Pro Gln Gly Glu Glu Asn Tyr Glu Trp Arg

50 55 60

Leu Arg Ser Val Pro Val Asn Ala Val Thr Asn Pro Lys Ser Ile Cys

65 70 75 80

Val Ile Ala Ala Gly Ser Glu Ile Asp Met Glu Val Leu Leu Ser Glu

85 90 95

Ile Phe Asp Leu Asn Ala Ala Gly Tyr Asn Ile Ser Glu Arg Leu Val

100 105 110

Ile Asp Gln Ser Ala Thr Met Leu Thr Gln Glu His His Ala Thr Glu

115 120 125

Leu Gly Arg Asn Met Gln Ala Gln Phe Gly Ser Thr Ser Lys Gly Ile

130 135 140

Gly Ala Ala Arg Ala Ala Arg Leu Met Arg Ser Ala Asp Leu Phe Gly

145 150 155 160

Gly Asp Val Asp Thr Ala Lys Met Leu Arg Asp His Leu Ala Val Gly

165 170 175

Gly Asp Val Val Ile Glu Gly Thr Gln Gly Tyr Gly Leu Gly Leu His

180 185 190

Ala Gly Glu Tyr Pro Phe Cys Thr Ser Gln Asp Cys Arg Ala Ile Asp

195 200 205

Phe Leu Gly Gln Ala Gly Leu Ser Pro Trp Asp Pro Ala Val Leu Asp

210 215 220

Phe Ser Val Ile Val Val Ala Arg Thr Tyr Pro Ile Arg Val Ala Gly

225 230 235 240

Asn Ser Gly Pro Leu Lys Asn Glu Thr Ser Trp Ser Glu Leu Gly Leu

245 250 255

Pro Glu Glu Phe Thr Thr Val Thr Arg Lys Val Arg Arg Val Gly Gln

260 265 270

Tyr Asp His Lys Leu Val Arg Asp Ala Val Ala Ala Asn Gly Gly Ala

275 280 285

Pro Val Val Gln Leu Ala Leu Thr Met Phe Asp Gln Val Phe Thr Asp

290 295 300

Leu Tyr Gly Gln Ala Gly Pro Leu Glu Leu Ser Gln Glu Gln Ser Asp

305 310 315 320

Phe Ile Asp Glu Ile Glu Glu Gly Ala Asn Ala Pro Val Ala Phe Ile

325 330 335

Gly Thr Ser Pro Thr Thr Ile Gly Trp Arg Ala

340 345

<210> 131

<211> 356

<212> PRT

<213> uncultured tailed phage (uncultured Caudovirales phase)

<400> 131

Met Thr Ile Asn Pro Ser Ala Ile His Cys Val Val Gly Gly Gln Phe

1 5 10 15

Gly Ser Glu Ala Lys Gly His Val Thr Ala Gln Leu Leu Lys Arg Leu

20 25 30

Tyr Gln Glu Asn Glu His Ala Pro Ile Asn Val Arg Val Gly Gly Ser

35 40 45

Asn Ala Gly His Ser Ala Ala Asn Tyr Val Asn Gly Ala Ile Ile Ala

50 55 60

Leu Arg Thr Ile Pro Ile Gly Ala Val Val Arg Pro Glu Ile Asp Leu

65 70 75 80

Val Ile Ala Ala Gly Ser Glu Ile Asp Pro Glu Val Leu Tyr Asn Glu

85 90 95

Ile Asp Leu Leu Glu Ser Tyr Gly Ile Pro Val Leu His Arg Leu Val

100 105 110

Ile Asp Lys Tyr Ala Thr Ile Ile Glu Pro His His Ile Asp Ser Glu

115 120 125

Gln Asn Ser Asp Leu Asn Ala Arg Thr Gly Ser Thr Asn Lys Gly Ile

130 135 140

Gly Ala Ser Arg Ala Ala Arg Leu Met Arg Gln Ala Thr Ile Ala Arg

145 150 155 160

Asp Trp Gln Phe Thr Arg Asp Ile Thr Val Ala Asp Thr Ser His Leu

165 170 175

Leu Asn His Thr Asn Arg Thr Ile Val Ile Glu Gly Thr Gln Gly Tyr

180 185 190

Gly Leu Gly Leu His Thr Glu Gln Tyr Pro Gln Thr Thr Ser Gly Asp

195 200 205

Cys Arg Ala Ile Asp Leu Ile Ala Gln Thr Gly Val Phe Pro Thr Pro

210 215 220

Thr Arg Pro Ile Glu Val Trp Leu Val Val Arg Thr Tyr Pro Ile Arg

225 230 235 240

Val Ala Gly Asn Ser Gly Lys Leu Thr Gln Glu Leu Thr Trp Glu Glu

245 250 255

Leu Asn Arg Arg Asn Ser Asn Ile Thr Pro Glu Tyr Thr Thr Val Thr

260 265 270

Lys Lys Gln Arg Arg Val Gly Glu Trp Asp Thr Ala Leu Val Arg Glu

275 280 285

Ala Ile Asn Ala Asn Gly Gly Thr Gly Ser His Met His Leu Cys Leu

290 295 300

Met Phe Ala Asp Tyr Ile Asp Glu Thr Leu Ala Thr Met Ser Glu Tyr

305 310 315 320

Glu Cys Leu Asp Met Pro Thr Ile Met Lys Leu Ala Glu Tyr Glu Thr

325 330 335

Asp Met Gly Gln Gln Cys Asp Met Tyr Gly Thr Ser Pro Tyr Ser Val

340 345 350

Ile Trp Thr Arg

355

<210> 132

<211> 379

<212> PRT

<213> Arthrobacter bacteriophage AppleCider (Arthrobacter phase AppleCider)

<400> 132

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Lys Leu Ala Val Lys

20 25 30

Ala Glu Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly His Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Asp Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu

85 90 95

Asp Gln Gly His Ile Leu Asp Leu Leu Ile Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Lys Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Ile Trp Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Leu Ala

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Arg Val Val Asp Thr Val Asp Tyr

165 170 175

Leu His Thr Ala Leu Gln Lys Pro Ser Val His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Ile Leu Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Asn

245 250 255

Glu Thr Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu His Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Glu Leu Val Ala

275 280 285

Glu Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Gly Glu Asp Asn Leu

290 295 300

Glu Ala Leu Leu Trp Glu Ala Val Gln Gly Gly Pro Ser Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Glu

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp

340 345 350

Ile Glu Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 133

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage LilStuart (Arthrobacter phase LilStuart)

<400> 133

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys Ser Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Ser Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Val Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr Leu His

165 170 175

Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn Glu Thr

245 250 255

Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 134

<211> 377

<212> PRT

<213> Arthrobacter phage Maria1952(Arthrobacter phage Maria1952)

<400> 134

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Arg Glu Ala Ala Arg His Asn

20 25 30

His Ser Ile Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Lys Gly His

85 90 95

Gly His Ile Leu Gln Leu Leu Val Asp Glu Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ser Glu Gly Gln Met Val Asp Arg Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Gln Leu Leu

145 150 155 160

Thr Glu Ile Ser Gly Val Lys Val Cys Asp Thr Val Ala Tyr Leu His

165 170 175

Gly Gln Ala Ser Arg Glu Glu Val Asn Ile Ile Val Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Ala Ala Val Gln Val Met Ile Ala Cys Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Glu Gly Glu Thr

245 250 255

Thr Trp Glu Glu Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Ala Ala Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Lys Ile Asp Glu Asp Asp Ile His Gly

290 295 300

Gln Leu Gln Leu Leu Val Ser Gly Gly Pro Lys Val Thr Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Val Pro Gly Ile Glu Gly Ala Thr Asp Ile

325 330 335

Asp Lys Ile Glu Pro Glu Glu Phe Ala Lys Val Glu Glu Trp Ile Glu

340 345 350

Lys Ile Tyr Arg Glu Thr Gly Ala His Thr Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Leu Leu Ile Gly Ala

370 375

<210> 135

<211> 406

<212> PRT

<213> Microbacterium phage Zanella (Microbacterium phage Zanella)

<400> 135

Met Gln Tyr Val Ser Thr Ile Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Lys Ala Ala Ala Lys Asp Ala

20 25 30

Arg Asp Tyr Ala Thr Glu His Asp Val Pro Ile Pro Glu Thr Ile Asn

35 40 45

Val Arg Val Ala Gly Pro Asn Ala Gly His Thr Val Tyr Asp Asp Arg

50 55 60

Gly Gln Lys Phe Ala Leu Arg Gln Ile Pro Val Gly Ala Val Tyr Glu

65 70 75 80

Asp Val Lys Leu Tyr Ile Ala Pro Gly Ser Glu Ile Asp Leu Asp Val

85 90 95

Leu Tyr Ser Glu Ile Glu Ala Leu Glu Ala Ala Gly His Pro Ile Gln

100 105 110

His Arg Leu Trp Ile Ser Arg Gln Ala Thr Val Ile Thr Gln Glu His

115 120 125

Lys Asp Ala Glu Ala Ala Leu Val Gly Gly Ile Gly Ser Thr Gly Lys

130 135 140

Gly Ile Gly Ala Ala Arg Ala Ala Arg Leu Leu Arg Ser Ala Glu Thr

145 150 155 160

Ile Gly Asp Tyr Met Asp Ala Ala Gly Leu Gly Thr Met Trp Glu Trp

165 170 175

Arg Glu Pro Ser Glu Trp Tyr Ala Ser Asp Asp Phe Val His Asp Asn

180 185 190

Leu Ser His Val Leu Ile Glu Gly Thr Gln Gly Tyr Gly Leu Ser Leu

195 200 205

Arg Ala Ser Gly Asn Tyr Pro Tyr Val Thr Ser Ser Asp Ala Arg Ala

210 215 220

Ile Asp Phe Met Ala Met Ala Gly Val Asp Pro Thr Arg Cys Ser Val

225 230 235 240

Lys Ala Thr Asn Trp Val Val Ala Arg Val Phe Pro Ile Arg Val Ala

245 250 255

Gly Asn Ser Gly Pro Met Lys Gly Glu Thr Ser Trp Asp Glu Leu Gly

260 265 270

Leu Pro Glu Glu Arg Thr Thr Val Thr Gln Lys Val Arg Arg Val Gly

275 280 285

Glu Phe Asp Val Asp Leu Leu Arg Glu Ala Val Gln Ala Asn Gly Gly

290 295 300

His Asn Ala Gln Val Val Ile Thr Met Leu Asp Gln Val Ile Pro Gly

305 310 315 320

Leu Ala Asp Val Asp Pro Asp Gln Ile His Asp Asp Glu Gly Thr Val

325 330 335

Asp Pro Ser Gln Ser Glu Tyr Leu Gln Glu Ala Leu Glu Trp Val Asn

340 345 350

Glu His Ala Gly Tyr Asp Lys Ile Gly Ala His Val Gly Ala Ile Thr

355 360 365

Phe Gly Pro Thr Lys Met Leu Phe Thr Asn His Gly Ala Asn Ala Asn

370 375 380

Asn Pro Gly Gly Gly Asp Gln Ala Met Val Asp Ala Ile Met Ser Gln

385 390 395 400

Ile Phe Gly Gly Gly Gln

405

<210> 136

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Huntingdon (Arthrobacter phage Huntingdon)

<400> 136

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Ile Thr Ala Gln Leu Val Lys Gln Ala Val Lys Ser Gly

20 25 30

Arg His Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Gln Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Ala Val Leu Val Glu Glu Ile His Leu Ala Gln Asp His

85 90 95

Gly His Val Ile Gln Leu Leu Ile Asp Glu Asn Ala Thr Leu Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ala Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Asp Arg Ile Trp

130 135 140

Arg Arg Ala Arg Arg Leu Arg Asp Ser Glu Pro Ala Leu Lys Leu Leu

145 150 155 160

Ala Asp Ile Ser Gly Val His Val Ile Asp Thr Val Lys Tyr Leu His

165 170 175

Gly Gln Ala Thr Gln Pro Asn Val Asn Ile Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Glu Ala Thr Gln Val Ile Ile Ala Cys Arg Val

225 230 235 240

Phe Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Gly Glu Thr

245 250 255

Ser Trp Glu Gln Leu Asn Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Gly Ala Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Ala Ile Asp His Asp Asp Met Glu Gly

290 295 300

Gln Leu Met Gln Leu Val Ser Gly Gly Pro Lys Val Met Val Gly Leu

305 310 315 320

Thr Met Leu Asp Gln Val Val Pro Glu Ile Glu Gly Leu Thr Thr Phe

325 330 335

Asp Asp Leu Asp Glu Pro Thr Phe Ser Lys Val Glu Glu Trp Ile Asn

340 345 350

Lys Ile Tyr Asp Glu Thr Gly Ala Gln Val Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Val Leu Leu Gly Ala

370 375

<210> 137

<211> 379

<212> PRT

<213> Arthrobacter bacteriophage Fluke (Arthrobacter phase Fluke)

<400> 137

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser

20 25 30

Ala Asp Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu

85 90 95

Asp His Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Ile Trp Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Thr

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr

165 170 175

Leu His Glu Ala Leu Gln Lys Pro Asn Ala His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn

245 250 255

Glu Thr Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala

275 280 285

Asp Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu

290 295 300

Glu Ala Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp

340 345 350

Ile Asp Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Val Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 138

<211> 379

<212> PRT

<213> Arthrobacter bacteriophage PitaDog (Arthrobacter phase PitaDog)

<400> 138

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Lys

20 25 30

Ser Asp Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Leu Asp Glu Ile His Leu Ala Leu

85 90 95

Asp His Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Val Trp Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Val Glu

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Arg Val His Asp Thr Val Gln Tyr

165 170 175

Leu His Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Thr Val Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Gln Asn

245 250 255

Glu Thr Ser Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala

275 280 285

Asp Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Asp Glu Glu Asn Leu

290 295 300

Glu Ala Leu Leu Trp Gln Ala Val Gln Gly Gly Pro His Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Thr Gly Leu Ser

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Ala Trp

340 345 350

Ile Asp Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 139

<211> 377

<212> PRT

<213> Arthrobacter phage Nubia (Arthrobacter phage Nubia)

<400> 139

Met Ser Asn Val Met Val Val Val Gly Gly Gln Tyr Gly Ser Glu Ala

1 5 10 15

Lys Gly His Ile Thr Ala Gln Leu Val Lys Gln Ala Val Gln Val Gly

20 25 30

Arg His Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Val Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Val Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Val Glu Glu Ile His Leu Ala Gln Asp Asn

85 90 95

Gly His Ile Ile Gln Leu Leu Ile Asp Glu Asn Ala Thr Leu Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Ser Glu Gly Lys Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Asp Arg Ile Trp

130 135 140

Arg Arg Ala Arg Arg Leu Arg Asp Ser Glu Ala Ala Leu Glu Leu Leu

145 150 155 160

Arg Gln Ile Ser Gly Val His Val Ile Asp Thr Val Lys Tyr Leu His

165 170 175

Gly Gln Ala Thr Gln Pro Asn Val Asn Ile Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp His Pro Gly Ile Glu Ala Thr Gln Val Ile Ile Ala Cys Arg Val

225 230 235 240

Phe Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Gly Glu Thr

245 250 255

Ser Trp Ala Gln Leu Asn Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Ala Trp Asp Gly Glu Leu Val Lys Ala Ala

275 280 285

Phe Glu Ala Asn Gly Gly Val Ala Ile Asp His Asp Asp Met Glu Gly

290 295 300

Gln Leu Met Gln Leu Val Ser Gly Gly Pro Lys Val Met Val Gly Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Thr Thr Phe

325 330 335

Asp Asp Leu Asp Glu Pro Thr Leu Ser Lys Val Glu Glu Trp Ile Asn

340 345 350

Lys Ile Tyr Asp Glu Thr Gly Ala Gln Val Ala Met Ile Thr Thr Ser

355 360 365

Pro Lys Thr Ala Val Leu Leu Gly Ala

370 375

<210> 140

<211> 379

<212> PRT

<213> Arthrobacter bacteriophage Dino (Arthrobacter phage Dino)

<400> 140

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser

20 25 30

Ala Asp Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu

85 90 95

Asp His Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Ile Trp Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Thr

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr

165 170 175

Leu His Glu Ala Leu Gln Lys Pro Asn Ala His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn

245 250 255

Glu Thr Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala

275 280 285

Asp Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu

290 295 300

Glu Ala Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp

340 345 350

Ile Asp Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Val Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 141

<211> 379

<212> PRT

<213> Arthrobacter bacteriophage Canowick (Arthrobacter phage Canovick)

<400> 141

Met Asp Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser

1 5 10 15

Glu Ala Lys Gly His Val Thr Ala Gln Leu Val Lys Leu Ala Val Lys

20 25 30

Ala Glu Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly

35 40 45

His Thr Ala Tyr Asp Asp Glu Gly His Lys Phe Ala Phe Arg Gln Val

50 55 60

Pro Val Gly Ala Val Ile Asp Pro Ile Thr Ser Val Ile Ala Ala Gly

65 70 75 80

Ser Glu Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu

85 90 95

Asp Gln Gly His Ile Leu Asp Leu Leu Ile Asp Gly Asn Ala Thr Met

100 105 110

Ile Glu Tyr His His Lys Met Gln Glu Gln Glu Gly Lys Met Val Glu

115 120 125

Asn Ile Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg

130 135 140

Ile Trp Arg Lys Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Leu Ala

145 150 155 160

Leu Leu Asn Gln Leu Pro Gly Val Arg Val Val Asp Thr Val Asp Tyr

165 170 175

Leu His Thr Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly

180 185 190

Thr Gln Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr

195 200 205

Thr Ser Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ser Gly Ile

210 215 220

Ser Pro Trp Gln Thr Gly Val Asp Thr Leu Gln Val Phe Ile Ala Ala

225 230 235 240

Arg Val Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Lys Asn

245 250 255

Glu Thr Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu His Thr Thr Val

260 265 270

Thr Gln Lys Val Arg Arg Val Gly Asp Trp Asp Gly Glu Leu Val Ala

275 280 285

Glu Ala Phe Arg Ala Asn Gly Gly Val Arg Ile Gly Glu Asp Asn Leu

290 295 300

Glu Ala Leu Leu Trp Glu Ala Val Gln Gly Gly Pro Ser Val Val Val

305 310 315 320

Ala Leu Thr Met Leu Asp Gln Val Ile Pro Glu Ile Glu Gly Leu Glu

325 330 335

Ser Phe Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp

340 345 350

Ile Glu Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala

355 360 365

Thr Ser Pro Lys Thr Val Val Leu Ile Gly Ala

370 375

<210> 142

<211> 377

<212> PRT

<213> Arthrobacter phage Scuttle (Arthrobacter phage Scuttle)

<400> 142

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 143

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage MrGlopy (Arthrobacter phase MrGlopy)

<400> 143

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 144

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage potatoes (Arthrobacter phage potatoes)

<400> 144

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Val Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Ala Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Val His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Ile Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 145

<211> 377

<212> PRT

<213> Arthrobacter bacteriophage Zorro (Arthrobacter phase Zorro)

<400> 145

Met Ser Asn Ile Ala Val Val Val Gly Gly Gln Phe Gly Ser Glu Ala

1 5 10 15

Lys Gly His Val Thr Ala Gln Leu Val Ala Leu Ala Ala Ser Ala Asp

20 25 30

Arg Glu Val Ile Asn Val Arg Val Ala Gly Pro Asn Ala Gly His Thr

35 40 45

Ala Tyr Asp Asp Glu Gly Asn Lys Phe Ala Phe Arg Gln Val Pro Val

50 55 60

Gly Ala Val Ile Glu Pro Ile Thr Ser Val Ile Ala Ala Gly Ser Glu

65 70 75 80

Ile Asp Leu Pro Val Leu Ile Glu Glu Ile His Leu Ala Leu Asp His

85 90 95

Gly His Ile Leu Asp Leu Leu Val Asp Gly Asn Ala Thr Met Ile Glu

100 105 110

Tyr His His Lys Met Gln Glu Gln Glu Gly Arg Met Val Glu Asn Ile

115 120 125

Gly Ser Thr Ala Lys Gly Ile Gly Ala Ala Arg Ala Glu Arg Ile Trp

130 135 140

Arg Thr Ala Arg Arg Leu Arg Asp Val Pro Glu Ala Met Thr Leu Leu

145 150 155 160

Asn Gln Leu Pro Gly Val Gln Val Ala Asp Thr Val Gly Tyr Leu His

165 170 175

Glu Ala Leu Gln Lys Pro Asn Ala His Val Ile Ile Glu Gly Thr Gln

180 185 190

Gly Tyr Gly Leu Gly Val His Thr Asp Ala Tyr Pro Gln Thr Thr Ser

195 200 205

Ser Asp Cys Arg Ala Ile Asp Phe Leu Ala Met Ala Gly Ile Ser Pro

210 215 220

Trp Gln Thr Gly Val Asp Val Val Gln Val Phe Ile Ala Ala Arg Val

225 230 235 240

Tyr Pro Ile Arg Val Ala Gly Asn Ser Gly Pro Met Asn Asn Glu Thr

245 250 255

Thr Trp Glu Ala Leu Gly Leu Pro Glu Glu Arg Thr Thr Val Thr Gln

260 265 270

Lys Val Arg Arg Val Gly Asp Trp Asp Gly Gln Leu Val Ala Asp Ala

275 280 285

Phe Arg Ala Asn Gly Gly Val Arg Ile Ser Glu Asp Asn Leu Glu Ala

290 295 300

Leu Leu Trp Gln Ala Val Glu Gly Gly Pro His Val Val Val Ala Leu

305 310 315 320

Thr Met Leu Asp Gln Val Ile Pro Glu Ile Ala Gly Leu Thr Ser Phe

325 330 335

Asp Asp Cys Asp Ala Ala Thr Leu Gln Lys Val Glu Glu Trp Ile Asp

340 345 350

Arg Val Tyr Arg Asp Thr Gly Ala Gln Val Lys Met Val Ala Thr Ser

355 360 365

Pro Lys Thr Val Val Arg Ile Gly Ala

370 375

<210> 146

<211> 359

<212> PRT

<213> cyanobacterial phage S-2L (Cyanophage S-2L)

<400> 146

Met Leu Ser Ile Pro Pro Tyr Tyr Arg Val Lys Asn Cys Asn Leu Ile

1 5 10 15

Val Asp Cys Gln Tyr Gly Ser Thr Gly Lys Gly Leu Leu Ala Gly Tyr

20 25 30

Leu Gly Ala Leu Glu Ala Pro Gln Val Leu Cys Met Ala Pro Ser Pro

35 40 45

Asn Ala Gly His Thr Leu Val Glu Glu Asp Gly Thr Ala Arg Val His

50 55 60

Lys Met Leu Pro Leu Gly Ile Thr Ser Pro Ser Leu Glu Arg Ile Tyr

65 70 75 80

Leu Gly Pro Gly Ser Val Ile Asp Met Asp Arg Leu Leu Glu Glu Tyr

85 90 95

Leu Ala Leu Pro Arg Gln Val Glu Leu Trp Val His Gln Asn Ala Ala

100 105 110

Val Val Leu Gln Glu His Arg Asp Glu Glu Ala Ala Gly Gly Leu Ala

115 120 125

Pro Gly Ser Thr Arg Ser Gly Ala Gly Ser Ala Phe Ile Ala Lys Ile

130 135 140

Arg Arg Arg Pro Gly Thr Leu Leu Phe Gly Glu Ala Val Arg Asp His

145 150 155 160

Pro Leu His Gly Val Val Arg Val Val Asp Thr Arg Thr Ala Gln Asp

165 170 175

Met Leu Phe Arg Thr Arg Ser Ile Gln Ala Glu Gly Cys Gln Gly Tyr

180 185 190

Ser Leu Ser Val His His Gly Ala Tyr Pro Tyr Cys Thr Ala Arg Asp

195 200 205

Val Thr Thr Ala Gln Leu Ile Ala Asp Cys Gly Leu Pro Tyr Asp Val

210 215 220

Ala Arg Ile Ala Arg Val Val Gly Ser Met Arg Thr Tyr Pro Ile Arg

225 230 235 240

Val Ala Asn Arg Pro Glu Ala Gly Glu Trp Ser Gly Pro Cys Tyr Pro

245 250 255

Asp Ser Val Glu Cys Gln Phe Ala Asp Leu Gly Leu Glu Gln Glu Tyr

260 265 270

Thr Thr Val Thr Lys Leu Pro Arg Arg Ile Phe Thr Phe Ser Ala Ile

275 280 285

Gln Ala His Glu Ala Ile Ala Gln Asn Gly Val Asp Glu Val Phe Leu

290 295 300

Asn Phe Ala Gln Tyr Pro Pro Ser Leu Gly Ala Leu Glu Asp Ile Leu

305 310 315 320

Asp Ala Ile Glu Ala Arg Ala Glu Val Thr Tyr Val Gly Phe Gly Pro

325 330 335

Lys Val Thr Asp Val Tyr His Thr Pro Thr Arg Ala Glu Leu Glu Gly

340 345 350

Leu Tyr Ala Arg Tyr Arg Arg

355

Claims

1. A polypeptide having 2-aminodeoxyadenylate succinate (ADAS) synthetase activity capable of catalyzing the formation of 2-aminodeoxyadenylate succinate with one or more of ATP, dATP, GTP, dGTP and dGTP as well as dGMP and Asp as substrates and having a catalytic motif of the polypeptide altered to GSxxKG compared to the GDxxKG catalytic motif of adenylate succinate synthetase (PurA), wherein x represents any amino acid residue.

2. The polypeptide according to claim 1, wherein position 303 corresponding to SEQ ID NO:72 is changed from R to L when the polypeptide is aligned with the amino acid sequence of adenylate succinate synthetase from Escherichia coli (SEQ ID NO: 72).

3. The polypeptide of claim 1 or 2, wherein the polypeptide has an amino acid sequence corresponding to T at position 274, N at position 306, F at position 307, and N at position 309 of SEQ ID No. 2 when aligned with the amino acid sequence shown in SEQ ID No. 2.

4. A polypeptide according to any of claims 1 to 3 comprising a sequence as set forth in any of SEQ ID NOs 1 to 4, 9 to 69, 71 and 92 to 146, or a variant of a sequence as set forth in any of SEQ ID NOs 1 to 4, 9 to 69, 71 and 92 to 146 which retains 2-aminodeoxyadenylate succinate (ADAS) synthetase activity with one or more insertions, deletions and/or substitutions of an amino acid, or a fragment of a sequence as set forth in any of SEQ ID NOs 1 to 4, 9 to 69, 71 and 92 to 146 which retains a catalytic motif.

5. Polypeptide having 2 '-deoxyadenine 5' -triphosphate triphosphatase (dATPase) activity capable of catalyzing the hydrolysis of dATP to 2 '-deoxyadenine (dA) and preferably capable of catalyzing the hydrolysis of dADP and dAMP to 2' -deoxyadenine (dA), comprising a metal and ligand binding pocket and preferably comprising Co ²⁺ As a divalent metal cofactor.

6. A polypeptide according to claim 5 comprising a sequence as set forth in any of SEQ ID NOs 5 to 7, or a variant of a sequence as set forth in any of SEQ ID NOs 5 to 7 and 73 to 91 which retains dATPase activity with one or more amino acid insertions, deletions and/or substitutions, or a fragment of a sequence as set forth in any of SEQ ID NOs 5 to 7 and 73 to 91 which retains a catalytic motif.

7. Polypeptide having dATP and dGTP pyrophosphohydrolase activity capable of catalyzing the hydrolysis of dATP to dAMP and dGTP to dGMP, comprising a metal and ligand binding pocket and preferably comprising Co ²⁺ As a divalent metal cofactor.

8. A polypeptide according to claim 7, which comprises the sequence shown in SEQ ID NO 8, or a variant of the sequence shown in SEQ ID NO 8 which retains dATP and dGTP pyrophosphate hydrolase activity with insertion, deletion and/or substitution of one or more amino acids, or a fragment of the sequence shown in SEQ ID NO 8 which retains the catalytic motif.

9. A nucleic acid molecule encoding the polypeptide of any one of claims 1-8.

10. A vector comprising the nucleic acid molecule of claim 9.

11. A method of engineering a bacteriophage comprising introducing into the genome of the bacteriophage a nucleic acid molecule encoding the polypeptide of any one of claims 1 to 4, such that the bacteriophage expresses the polypeptide of any one of claims 1 to 4.

12. The method of claim 11, further comprising introducing a nucleic acid molecule encoding the polypeptide of any one of claims 5-6 into the genome of the bacteriophage to express the polypeptide of any one of claims 5-6 with the bacteriophage; and/or introducing a nucleic acid molecule encoding the polypeptide of any one of claims 7-8 into the genome of said bacteriophage, such that said bacteriophage expresses the polypeptide of any one of claims 7-8.

13. The method of claim 11 or 12, further comprising introducing a nucleic acid molecule encoding an adenylosuccinate lyase (PurB) into the genome of the bacteriophage, such that the bacteriophage expresses the adenylosuccinate lyase (PurB); and/or introducing a nucleic acid molecule encoding a GMP Kinase (GK) into the genome of the bacteriophage, such that the bacteriophage expresses a GMP Kinase (GK).

14. Bacteriophage obtained by the method of any one of claims 11 to 13.

15. A host cell, such as a bacterial cell, comprising the bacteriophage of claim 14.

16. Use of a bacteriophage of claim 14 or a host cell of claim 15 in diaminopurine deoxyribonucleotide (dZTP) synthesis, DNA origami, DNA-based data storage, antimicrobial drug manufacture, antimicrobial manufacture, or preservative manufacture.