Species | Enterococcus_B hirae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_B; Enterococcus_B hirae | |||||||||||
CAZyme ID | MGYG000004798_00646 | |||||||||||
CAZy Family | GH25 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 440496; End: 441527 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH25 | 6 | 165 | 6.8e-33 | 0.96045197740113 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06417 | GH25_LysA-like | 1.80e-40 | 21 | 179 | 19 | 195 | LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis. |
pfam01183 | Glyco_hydro_25 | 4.97e-30 | 6 | 167 | 1 | 176 | Glycosyl hydrolases family 25. |
cd00599 | GH25_muramidase | 5.87e-28 | 4 | 172 | 1 | 186 | Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity. |
cd06524 | GH25_YegX-like | 8.48e-23 | 6 | 174 | 3 | 194 | YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins. |
cd06525 | GH25_Lyc-like | 5.94e-20 | 6 | 165 | 3 | 169 | Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ASV81999.1 | 9.79e-259 | 1 | 343 | 1 | 343 |
QQY21739.1 | 3.30e-144 | 1 | 340 | 1 | 345 |
AFM69104.1 | 3.30e-144 | 1 | 340 | 1 | 345 |
QKX74311.1 | 1.46e-140 | 1 | 340 | 1 | 345 |
APB31733.1 | 1.63e-60 | 3 | 187 | 2 | 186 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5A6S_A | 1.03e-08 | 4 | 163 | 23 | 184 | Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1] |
2WAG_A | 4.88e-07 | 28 | 182 | 44 | 216 | TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames] |
1OBA_A | 9.77e-06 | 6 | 170 | 9 | 184 | ChainA, Lysozyme [Streptococcus phage Cp1] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000078 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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