Species | Blautia sp900765525 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp900765525 | |||||||||||
CAZyme ID | MGYG000002756_01084 | |||||||||||
CAZy Family | GH25 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 24722; End: 25807 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH25 | 6 | 183 | 3.7e-46 | 0.9943502824858758 |
CBM50 | 265 | 308 | 9.1e-18 | 0.975 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06414 | GH25_LytC-like | 7.28e-84 | 5 | 193 | 3 | 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 | 6.77e-34 | 5 | 191 | 2 | 185 | 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 | 7.49e-30 | 6 | 183 | 1 | 180 | Glycosyl hydrolases family 25. |
cd06413 | GH25_muramidase_1 | 9.84e-27 | 5 | 190 | 5 | 187 | Uncharacterized bacterial muramidase containing 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. |
cd06525 | GH25_Lyc-like | 3.43e-25 | 4 | 191 | 1 | 183 | 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 |
---|---|---|---|---|---|
QEK16471.1 | 4.00e-108 | 1 | 360 | 1 | 325 |
QYX27151.1 | 1.28e-101 | 1 | 360 | 1 | 325 |
QHB23957.1 | 6.43e-77 | 1 | 255 | 1 | 265 |
QEI31463.1 | 6.43e-77 | 1 | 255 | 1 | 265 |
QRT30197.1 | 6.43e-77 | 1 | 255 | 1 | 265 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4B8V_A | 2.19e-19 | 212 | 358 | 43 | 214 | ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva] |
2WAG_A | 2.16e-14 | 3 | 185 | 16 | 196 | TheStructure of a family 25 Glycosyl hydrolase from Bacillus anthracis. [Bacillus anthracis str. Ames] |
2WW5_A | 1.51e-12 | 6 | 193 | 272 | 468 | 3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6] |
2WWC_A | 2.02e-12 | 6 | 193 | 272 | 468 | 3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6] |
3HMC_A | 5.63e-11 | 6 | 190 | 8 | 177 | Endolysinfrom Bacillus anthracis [Bacillus anthracis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q49UX4 | 1.27e-30 | 213 | 361 | 29 | 194 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1 |
Q5HRU2 | 3.03e-27 | 200 | 360 | 16 | 190 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1 |
Q8CMN2 | 3.03e-27 | 200 | 360 | 16 | 190 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1 |
Q7A1T4 | 4.98e-27 | 197 | 361 | 13 | 202 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MW2) OX=196620 GN=sle1 PE=3 SV=1 |
Q7A7E0 | 4.98e-27 | 197 | 361 | 13 | 202 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain N315) OX=158879 GN=sle1 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000037 | 0.000008 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.