| Species | Yersinia massiliensis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Yersinia; Yersinia massiliensis | |||||||||||
| CAZyme ID | MGYG000002465_01436 | |||||||||||
| CAZy Family | GH104 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 11383; End: 11841 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH104 | 3 | 147 | 3e-60 | 0.9793103448275862 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd00736 | lambda_lys-like | 2.54e-83 | 5 | 149 | 1 | 141 | Bacteriophage lambda lysozyme and similar proteins. Lysozyme from bacteriophage lambda hydrolyzes the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), as do other lysozymes. However, unlike other lysozymes, bacteriophage lambda does not produce a reducing end upon cleavage of the peptidoglycan, but rather uses the 6-OH of the same MurNAc residue to produce a 1,6-anhydromuramic acid terminal residue and is therefore a lytic transglycosylase. An identical 1,6-anhydro bond is formed in bacterial peptidoglycans by the action of the lytic transglycosylases of E. coli, though they differ structurally. |
| COG4678 | COG4678 | 3.99e-72 | 4 | 152 | 27 | 179 | Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: prophages, transposons]. |
| pfam00959 | Phage_lysozyme | 1.26e-20 | 30 | 136 | 1 | 105 | Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin. |
| cd00442 | Lyz-like | 6.46e-05 | 54 | 96 | 17 | 59 | lysozyme-like domains. This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ALX94650.1 | 1.27e-82 | 1 | 152 | 1 | 152 |
| QDL31298.1 | 2.36e-74 | 3 | 152 | 4 | 155 |
| QFH71058.1 | 5.26e-74 | 3 | 149 | 4 | 151 |
| QGH63416.1 | 1.87e-73 | 1 | 152 | 1 | 154 |
| QDX21429.1 | 2.14e-73 | 5 | 151 | 12 | 158 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1D9U_A | 1.14e-66 | 1 | 151 | 2 | 153 | ChainA, Bacteriophage Lambda Lysozyme [Lambdavirus lambda],1D9U_B Chain B, Bacteriophage Lambda Lysozyme [Lambdavirus lambda],3D3D_A Chain A, Lysozyme [Lambdavirus lambda],3D3D_B Chain B, Lysozyme [Lambdavirus lambda] |
| 1AM7_A | 1.11e-60 | 1 | 151 | 2 | 153 | ChainA, LYSOZYME [Lambdavirus lambda],1AM7_B Chain B, LYSOZYME [Lambdavirus lambda],1AM7_C Chain C, LYSOZYME [Lambdavirus lambda] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P03706 | 7.11e-66 | 1 | 151 | 2 | 153 | Endolysin OS=Escherichia phage lambda OX=10710 GN=R PE=1 SV=1 |
| P51771 | 7.62e-48 | 5 | 152 | 8 | 165 | Endolysin OS=Escherichia phage P2 OX=10679 GN=K PE=3 SV=1 |
| 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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