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CAZyme Information: MGYG000000234_00652

You are here: Home > Sequence: MGYG000000234_00652

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 teuberi
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Vagococcaceae; Vagococcus; Vagococcus teuberi
CAZyme ID MGYG000000234_00652
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
814 MGYG000000234_1|CGC5 92386.48 9.1362
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000234 2257969 Isolate China Asia
Gene Location Start: 673640;  End: 676084  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000234_00652.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 131 309 8.1e-36 0.9717514124293786

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06522 GH25_AtlA-like 6.99e-63 128 326 1 192
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.
pfam01183 Glyco_hydro_25 4.77e-36 131 296 1 163
Glycosyl hydrolases family 25.
cd00599 GH25_muramidase 9.21e-23 130 293 2 157
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.
cd06415 GH25_Cpl1-like 1.90e-16 130 253 3 123
Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage.
cd06525 GH25_Lyc-like 8.99e-15 131 253 3 119
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCA29269.1 2.37e-167 90 812 146 856
QDJ05477.1 2.72e-59 126 331 62 263
QKR95814.1 5.21e-59 126 331 62 263
ANU73836.1 5.21e-59 126 331 62 263
ASU25886.1 5.21e-59 126 331 62 263

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1H09_A 8.57e-06 130 306 7 177
ChainA, LYSOZYME [Streptococcus phage Cp1]
2IXU_A 8.60e-06 130 306 8 178
ChainA, LYSOZYME [Streptococcus phage Cp1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P19385 9.59e-10 130 306 8 178
Lysozyme OS=Streptococcus phage Cp-7 OX=10748 GN=CPL7 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.001016 0.998013 0.000402 0.000197 0.000187 0.000170

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000234_00652.