Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s5078_1V6.1 |
Family | GH25 |
Protein Properties | Length: 185 Molecular Weight: 20454.9 Isoelectric Point: 5.2798 |
Chromosome | Chromosome/Scaffold: 5078 Start: 112 End: 666 |
Description | |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH25 | 10 | 104 | 1.1e-25 |
AFKLPFVLDIETKEGQTRARISQIVNTWGTQFKQRTGRTLMIYTFPSFIDSYLDSSLGSYPLWYAYYSSGTPANKAGWKAWEFIQYTNKGKVPGI |
Full Sequence |
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Protein Sequence Length: 185 Download |
VIESAGGLSA FKLPFVLDIE TKEGQTRARI SQIVNTWGTQ FKQRTGRTLM IYTFPSFIDS 60 YLDSSLGSYP LWYAYYSSGT PANKAGWKAW EFIQYTNKGK VPGISGDVDL NEYKGSEAEL 120 MAAYSNPTPN TSETAPQWKE SGRQWLIDQV GISSDWKAED PVDIGTLGSI LLKYTQNVLG 180 KKQS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06412 | GH25_CH-type | 9.0e-18 | 2 | 120 | 129 | + 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. | ||
pfam01183 | Glyco_hydro_25 | 8.0e-18 | 4 | 104 | 103 | + Glycosyl hydrolases family 25. | ||
cd06525 | GH25_Lyc-like | 3.0e-24 | 13 | 113 | 101 | + 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. | ||
cd06524 | GH25_YegX-like | 1.0e-24 | 13 | 115 | 106 | + 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. | ||
cd00599 | GH25_muramidase | 3.0e-26 | 13 | 113 | 103 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0003796 | lysozyme activity |
GO:0009253 | peptidoglycan catabolic process |
GO:0016998 | cell wall macromolecule catabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBA18122.1 | 2e-20 | 2 | 128 | 90 | 226 | putative glycoside hydrolase [Paenibacillus phage phiBP] |
RefSeq | XP_001786760.1 | 0 | 1 | 184 | 1 | 184 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | YP_694826.1 | 2e-18 | 7 | 142 | 90 | 227 | glycosy hydrolase family protein [Clostridium perfringens ATCC 13124] |
RefSeq | ZP_02630442.1 | 2e-18 | 7 | 114 | 90 | 197 | glycosyl hydrolase, family 25 [Clostridium perfringens E str. JGS1987] |
RefSeq | ZP_02863939.1 | 2e-18 | 7 | 142 | 90 | 227 | glycosyl hydrolase, family 25 [Clostridium perfringens C str. JGS1495] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1jfx_A | 0.000000000000009 | 13 | 126 | 93 | 215 | A Chain A, Crystal Structure Of The Bacterial Lysozyme From Streptomyces Coelicolor At 1.65 A Resolution |
PDB | 2wag_A | 0.0005 | 13 | 120 | 100 | 213 | A Chain A, The Structure Of A Family 25 Glycosyl Hydrolase From Bacillus Anthracis |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CA760394 | 116 | 13 | 120 | 0.024 |
HO517175 | 110 | 1 | 99 | 2.6 |
CI540259 | 33 | 67 | 99 | 8.3 |
Orthologous Group | |||||
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Species | ID | ||||
Selaginella moellendorffii | 98236 | 98567 |
Sequence Alignments (This image is cropped. Click for full image.) |
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