Species | Aeromonas dhakensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Aeromonadaceae; Aeromonas; Aeromonas dhakensis | |||||||||||
CAZyme ID | MGYG000001692_01592 | |||||||||||
CAZy Family | GH24 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 191312; End: 191788 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH24 | 4 | 137 | 7.8e-16 | 0.8686131386861314 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00735 | T4-like_lys | 3.99e-56 | 3 | 154 | 1 | 146 | bacteriophage T4-like lysozymes. Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium. |
PHA02596 | 5 | 2.94e-19 | 3 | 150 | 174 | 331 | baseplate hub subunit and tail lysozyme; Provisional |
cd00737 | lyz_endolysin_autolysin | 3.99e-05 | 7 | 37 | 4 | 34 | endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan. |
cd16902 | pesticin_lyz | 2.36e-04 | 82 | 145 | 116 | 176 | lysozyme-like C-terminal domain of pesticin. Pesticin (Pst) is an anti-bacterial toxin produced by Yersinia pestis that acts through uptake by the target related bacteria and the hydrolysis of peptidoglycan in the periplasm. Pst contains an N-terminal translocation domain, an intermediate receptor binding domain, and a phage-lysozyme like C-terminal activity domain. Bacteriocins such as pesticin are produced by gram-negative bacteria to attack related bacterial stains. Pst is transported to the periplasm via FyuA, an outer-membrane receptor of Y. pestis and E. coli, where it hydrolyzes peptidoglycan via the cleavage of N-acetylmuramic acid and C4 of N-acetylglucosamine. Disruption of the peptidoglycan layer renders the bacteria vulnerable to lysis via osmotic pressure. The pesticin C-terminal domain resembles the lysozyme-like family, which includes soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, and chitosanases. All the members are involved in the hydrolysis of beta-1,4- linked polysaccharides. |
cd16901 | lyz_P1 | 0.002 | 12 | 37 | 14 | 39 | P1 lysozyme Lyz-like proteins. Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AVQ86204.1 | 1.96e-77 | 1 | 157 | 1 | 155 |
QDH46539.1 | 2.85e-61 | 1 | 156 | 6 | 157 |
QEG09029.1 | 3.45e-61 | 1 | 156 | 1 | 152 |
QDH46775.1 | 4.05e-61 | 1 | 156 | 6 | 157 |
QDH46919.1 | 8.16e-61 | 1 | 156 | 6 | 157 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2B7X_A | 5.76e-20 | 3 | 152 | 2 | 164 | ChainA, Lysozyme [Tequatrovirus T4],2B7X_B Chain B, Lysozyme [Tequatrovirus T4],2B7X_C Chain C, Lysozyme [Tequatrovirus T4],2B7X_D Chain D, Lysozyme [Tequatrovirus T4] |
1QTZ_A | 1.40e-19 | 3 | 152 | 2 | 158 | ChainA, PROTEIN (T4 LYSOZYME) [Tequatrovirus T4] |
1ZYT_A | 3.90e-19 | 3 | 152 | 2 | 158 | ChainA, Lysozyme [Escherichia phage T4] |
137L_A | 5.49e-19 | 3 | 152 | 2 | 158 | ChainA, T4 LYSOZYME [Tequatrovirus T4],137L_B Chain B, T4 LYSOZYME [Tequatrovirus T4] |
190L_A | 7.72e-19 | 3 | 152 | 2 | 158 | ChainA, LYSOZYME [Tequatrovirus T4] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P00720 | 4.10e-14 | 3 | 152 | 2 | 158 | Endolysin OS=Enterobacteria phage T4 OX=10665 GN=E PE=1 SV=2 |
Q556F2 | 4.62e-14 | 1 | 150 | 2 | 164 | Probable T4-type lysozyme 1 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0274831 PE=3 SV=1 |
Q86AA1 | 2.85e-09 | 1 | 150 | 2 | 164 | Probable T4-type lysozyme 2 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0274291 PE=2 SV=1 |
P16009 | 9.89e-08 | 3 | 150 | 175 | 334 | Pre-baseplate central spike protein Gp5 OS=Enterobacteria phage T4 OX=10665 GN=5 PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000038 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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