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CAZyme Information: MGYG000002299_00572

You are here: Home > Sequence: MGYG000002299_00572

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Vagococcus sp003462485
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Vagococcaceae; Vagococcus; Vagococcus sp003462485
CAZyme ID MGYG000002299_00572
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
266 MGYG000002299_1|CGC4 30758.84 6.9655
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002299 2039592 Isolate China Asia
Gene Location Start: 552009;  End: 552809  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002299_00572.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 5 164 5.7e-38 0.96045197740113

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06417 GH25_LysA-like 2.38e-49 2 178 1 195
LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
cd00599 GH25_muramidase 1.87e-39 3 171 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.
pfam01183 Glyco_hydro_25 4.49e-34 5 166 1 176
Glycosyl hydrolases family 25.
cd06525 GH25_Lyc-like 1.67e-32 3 164 1 169
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 1.32e-25 5 173 3 194
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
APB31733.1 3.43e-193 1 266 1 266
QNN73753.1 2.39e-126 1 265 1 262
QIL47414.1 7.67e-125 1 266 1 263
ASV81999.1 1.59e-61 2 186 3 187
QQY21739.1 5.30e-60 2 186 3 187

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000052 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002299_00572.