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endolysin [Bacillus phage Deep-Purple]
glycoside hydrolase family 25 protein( domain architecture ID 10158183)
glycoside hydrolase family 25 protein similar to PlyB, a bacteriophage endolysin active against Bacillus anthracis; endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues
List of domain hits
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Name | Accession | Description | Interval | E-value | ||||
GH25_PlyB-like | cd06523 | PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ... |
3-173 | 1.62e-80 | ||||
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. : Pssm-ID: 119383 Cd Length: 177 Bit Score: 239.96 E-value: 1.62e-80
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YraI super family | cl28549 | Uncharacterized conserved protein YraI [Function unknown]; |
190-257 | 4.71e-04 | ||||
Uncharacterized conserved protein YraI [Function unknown]; The actual alignment was detected with superfamily member COG4991: Pssm-ID: 444015 [Multi-domain] Cd Length: 92 Bit Score: 38.51 E-value: 4.71e-04
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Name | Accession | Description | Interval | E-value | ||||
GH25_PlyB-like | cd06523 | PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ... |
3-173 | 1.62e-80 | ||||
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. Pssm-ID: 119383 Cd Length: 177 Bit Score: 239.96 E-value: 1.62e-80
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Acm | COG3757 | Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ... |
3-179 | 4.71e-44 | ||||
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442971 Cd Length: 208 Bit Score: 147.74 E-value: 4.71e-44
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Glyco_hydro_25 | pfam01183 | Glycosyl hydrolases family 25; |
6-167 | 1.12e-21 | ||||
Glycosyl hydrolases family 25; Pssm-ID: 426105 Cd Length: 180 Bit Score: 88.96 E-value: 1.12e-21
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YraI | COG4991 | Uncharacterized conserved protein YraI [Function unknown]; |
190-257 | 4.71e-04 | ||||
Uncharacterized conserved protein YraI [Function unknown]; Pssm-ID: 444015 [Multi-domain] Cd Length: 92 Bit Score: 38.51 E-value: 4.71e-04
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Name | Accession | Description | Interval | E-value | ||||
GH25_PlyB-like | cd06523 | PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ... |
3-173 | 1.62e-80 | ||||
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. Pssm-ID: 119383 Cd Length: 177 Bit Score: 239.96 E-value: 1.62e-80
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Acm | COG3757 | Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ... |
3-179 | 4.71e-44 | ||||
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 442971 Cd Length: 208 Bit Score: 147.74 E-value: 4.71e-44
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GH25_muramidase | cd00599 | Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan ... |
3-173 | 2.34e-33 | ||||
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. Pssm-ID: 119373 [Multi-domain] Cd Length: 186 Bit Score: 119.76 E-value: 2.34e-33
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GH25_LytC-like | cd06414 | The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves ... |
2-173 | 4.41e-24 | ||||
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. Pssm-ID: 119376 Cd Length: 191 Bit Score: 95.33 E-value: 4.41e-24
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Glyco_hydro_25 | pfam01183 | Glycosyl hydrolases family 25; |
6-167 | 1.12e-21 | ||||
Glycosyl hydrolases family 25; Pssm-ID: 426105 Cd Length: 180 Bit Score: 88.96 E-value: 1.12e-21
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GH25_muramidase_1 | cd06413 | Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ... |
5-177 | 5.41e-14 | ||||
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. Pssm-ID: 119375 Cd Length: 191 Bit Score: 68.46 E-value: 5.41e-14
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GH25_YegX-like | cd06524 | YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) ... |
6-170 | 6.45e-13 | ||||
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. Pssm-ID: 119384 Cd Length: 194 Bit Score: 65.44 E-value: 6.45e-13
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GH25_Lyc-like | cd06525 | Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by ... |
3-173 | 1.90e-12 | ||||
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. Pssm-ID: 119385 Cd Length: 184 Bit Score: 63.85 E-value: 1.90e-12
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GH25_AtlA-like | cd06522 | AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell ... |
6-145 | 2.07e-08 | ||||
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain. Pssm-ID: 119382 Cd Length: 192 Bit Score: 52.76 E-value: 2.07e-08
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GH25_CH-type | cd06412 | CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of ... |
5-178 | 3.05e-04 | ||||
CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases. Pssm-ID: 119374 Cd Length: 199 Bit Score: 40.77 E-value: 3.05e-04
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YraI | COG4991 | Uncharacterized conserved protein YraI [Function unknown]; |
190-257 | 4.71e-04 | ||||
Uncharacterized conserved protein YraI [Function unknown]; Pssm-ID: 444015 [Multi-domain] Cd Length: 92 Bit Score: 38.51 E-value: 4.71e-04
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Blast search parameters | ||||
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