Species | Enterocloster sp900555045 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster sp900555045 | |||||||||||
CAZyme ID | MGYG000002995_00168 | |||||||||||
CAZy Family | GH25 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 4887; End: 6092 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH25 | 35 | 209 | 7.9e-50 | 0.9943502824858758 |
CBM50 | 299 | 342 | 1.3e-16 | 0.975 |
CBM50 | 239 | 282 | 5.5e-16 | 0.975 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06525 | GH25_Lyc-like | 1.10e-86 | 34 | 218 | 2 | 184 | 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. |
cd00599 | GH25_muramidase | 1.84e-54 | 33 | 218 | 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. |
cd06414 | GH25_LytC-like | 8.34e-51 | 34 | 218 | 3 | 190 | 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. |
pfam01183 | Glyco_hydro_25 | 2.00e-49 | 35 | 209 | 1 | 180 | Glycosyl hydrolases family 25. |
COG3757 | Acm | 5.41e-44 | 31 | 222 | 62 | 257 | Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ASN94242.1 | 1.40e-134 | 1 | 342 | 1 | 338 |
QRP41080.1 | 1.40e-134 | 1 | 342 | 1 | 338 |
QJU21453.1 | 1.61e-133 | 1 | 342 | 1 | 338 |
QJS18123.1 | 1.04e-123 | 33 | 400 | 34 | 397 |
QIB56830.1 | 7.21e-115 | 32 | 399 | 34 | 402 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4KRU_A | 8.96e-44 | 34 | 227 | 22 | 216 | X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101] |
4KRT_A | 2.12e-42 | 34 | 227 | 22 | 216 | X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101] |
4B8V_A | 5.34e-21 | 233 | 401 | 39 | 218 | ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva] |
1JFX_A | 1.73e-18 | 34 | 221 | 7 | 205 | Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor] |
2X8R_A | 2.67e-11 | 34 | 202 | 6 | 186 | Thestructure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_B The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_C The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_D The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_E The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293],2X8R_F The structure of a family GH25 lysozyme from Aspergillus fumigatus [Aspergillus fumigatus Af293] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P26836 | 3.43e-41 | 28 | 223 | 5 | 201 | Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2 |
P34020 | 6.95e-36 | 34 | 223 | 3 | 185 | Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1 |
Q6GJK9 | 2.73e-23 | 239 | 397 | 29 | 199 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=sle1 PE=3 SV=1 |
Q5HIL2 | 3.74e-23 | 239 | 397 | 29 | 199 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain COL) OX=93062 GN=sle1 PE=3 SV=1 |
Q7A1T4 | 3.74e-23 | 239 | 397 | 29 | 199 | N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus aureus (strain MW2) OX=196620 GN=sle1 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000272 | 0.999007 | 0.000192 | 0.000183 | 0.000160 | 0.000145 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.