Species | UMGS1696 sp900763885 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS1696; UMGS1696 sp900763885 | |||||||||||
CAZyme ID | MGYG000002123_00440 | |||||||||||
CAZy Family | GH25 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 337; End: 1122 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH25 | 6 | 190 | 1.5e-36 | 0.9943502824858758 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06414 | GH25_LytC-like | 2.22e-68 | 3 | 200 | 1 | 191 | The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes. |
cd00599 | GH25_muramidase | 1.82e-25 | 4 | 199 | 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. |
pfam01183 | Glyco_hydro_25 | 3.46e-19 | 6 | 190 | 1 | 180 | Glycosyl hydrolases family 25. |
pfam08230 | CW_7 | 1.04e-17 | 221 | 260 | 1 | 40 | CW_7 repeat. This domain was originally found in the C-terminal moiety of the Cpl-7 lysozyme encoded by the Streptococcus pneumoniae bacteriophage Cp-7. It is also found in the cell wall hydrolases of human and life-stock pathogens. CW_7 repeats make up a cell wall binding motif. |
smart01095 | Cpl-7 | 8.66e-16 | 220 | 260 | 1 | 41 | Cpl-7 lysozyme C-terminal domain. This domain was originally found in the C-terminal moiety of the Cpl-7 lysozyme encoded by the Streptococcus pneumoniae bacteriophage Cp-7. It is assumed that these repeats represent cell wall binding motifs although no direct evidence has been obtained so far. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QDS38460.1 | 1.24e-44 | 1 | 260 | 1 | 265 |
ASD51116.1 | 1.24e-44 | 1 | 260 | 1 | 265 |
AMC93674.1 | 3.47e-44 | 1 | 260 | 1 | 265 |
QBE96747.1 | 4.88e-44 | 1 | 260 | 1 | 265 |
QBX31317.1 | 4.88e-44 | 1 | 260 | 1 | 265 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P19385 | 2.01e-07 | 61 | 257 | 55 | 242 | Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000086 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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