Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 98236 |
Family | GH25 |
Protein Properties | Length: 264 Molecular Weight: 29356.9 Isoelectric Point: 7.2735 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH25 | 54 | 245 | 0 |
MDVSSYQGNVDWPSAYNNVARFAYIKGTEGTGYPNPYFSQQYVGSYRAGFIRGAYHFGRPDISNGATQAMYFLTNGGRWSSDGQTLPGALDIEYNPSCGN SCNPLQTCYNLGKPEMRKWIQDFVNTSKQGTGVYPVIYSTADWYNTCVGTYGDFSSVCPFWLACYCPMVTTYPYNWKVYTFWQYADSGTFPG |
Full Sequence |
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Protein Sequence Length: 264 Download |
MVFHCLIFPF LLLSFLSIPA QSFSLNTSDL YTHECHGLTA GRTLLQARSG VPGMDVSSYQ 60 GNVDWPSAYN NVARFAYIKG TEGTGYPNPY FSQQYVGSYR AGFIRGAYHF GRPDISNGAT 120 QAMYFLTNGG RWSSDGQTLP GALDIEYNPS CGNSCNPLQT CYNLGKPEMR KWIQDFVNTS 180 KQGTGVYPVI YSTADWYNTC VGTYGDFSSV CPFWLACYCP MVTTYPYNWK VYTFWQYADS 240 GTFPGDQNVF NGPYSLLQKL AKG* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06524 | GH25_YegX-like | 2.0e-36 | 53 | 252 | 212 | + 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. | ||
cd06413 | GH25_muramidase_1 | 5.0e-38 | 51 | 252 | 209 | + 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. | ||
cd00599 | GH25_muramidase | 1.0e-45 | 53 | 250 | 203 | + 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 | 6.0e-47 | 55 | 246 | 192 | + Glycosyl hydrolases family 25. | ||
cd06412 | GH25_CH-type | 7.0e-90 | 51 | 257 | 207 | + 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. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | YP_001109221.1 | 0 | 28 | 263 | 12 | 235 | lysozyme M1 precursor [Saccharopolyspora erythraea NRRL 2338] |
RefSeq | YP_003135565.1 | 0 | 46 | 263 | 80 | 287 | lysozyme M1 (1,4-beta-N-acetylmuramidase) [Saccharomonospora viridis DSM 43017] |
RefSeq | ZP_05480457.1 | 0 | 51 | 263 | 41 | 246 | lysozyme precursor [Streptomyces sp. AA4] |
RefSeq | ZP_06215515.1 | 0 | 52 | 261 | 41 | 243 | glycoside hydrolase family 25 [Micromonospora aurantiaca ATCC 27029] |
RefSeq | ZP_06397952.1 | 0 | 52 | 261 | 41 | 243 | glycoside hydrolase family 25 [Micromonospora sp. L5] |
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 | 2x8r_F | 0 | 51 | 263 | 4 | 210 | A Chain A, The Structure Of A Family Gh25 Lysozyme From Aspergillus Fumigatus |
PDB | 2x8r_E | 0 | 51 | 263 | 4 | 210 | A Chain A, The Structure Of A Family Gh25 Lysozyme From Aspergillus Fumigatus |
PDB | 2x8r_D | 0 | 51 | 263 | 4 | 210 | A Chain A, The Structure Of A Family Gh25 Lysozyme From Aspergillus Fumigatus |
PDB | 2x8r_C | 0 | 51 | 263 | 4 | 210 | A Chain A, The Structure Of A Family Gh25 Lysozyme From Aspergillus Fumigatus |
PDB | 2x8r_B | 0 | 51 | 263 | 4 | 210 | A Chain A, The Structure Of A Family Gh25 Lysozyme From Aspergillus Fumigatus |
Signal Peptide | |||||
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Cleavage Site | |||||
22 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO532404 | 212 | 53 | 263 | 0 |
CA760394 | 201 | 64 | 264 | 0 |
CA760394 | 201 | 64 | 264 | 0 |
HO532404 | 212 | 53 | 263 | 0 |
HO517175 | 145 | 93 | 237 | 2.99878e-43 |
Orthologous Group | |||||
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Species | ID | ||||
Physcomitrella patens | Pp1s5078_1V6.1 | ||||
Selaginella moellendorffii | 98567 |
Sequence Alignments (This image is cropped. Click for full image.) |
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