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CAZyme Information: MGYG000002549_01890

You are here: Home > Sequence: MGYG000002549_01890

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 Bacteroides caccae
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides caccae
CAZyme ID MGYG000002549_01890
CAZy Family GH24
CAZyme Description Lysozyme RrrD
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
144 16041.56 10.0069
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002549 5479119 Isolate United States North America
Gene Location Start: 972343;  End: 972777  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002549_01890.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH24 9 135 1.2e-44 0.948905109489051

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00737 lyz_endolysin_autolysin 4.41e-65 11 140 5 136
endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
cd16901 lyz_P1 5.63e-48 11 135 10 135
P1 lysozyme Lyz-like proteins. Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
cd16900 endolysin_R21-like 1.03e-37 11 135 12 137
endolysin R21-like proteins. Unlike T4 E phage lysozyme, the endolysin R21 from Enterobacteria phage P21 has an N-terminal SAR (signal-arrest-release) domain that anchors the endolysin to the membrane in an inactive form, which act to prevent premature lysis of the infected bacterium. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
COG3772 RrrD 3.32e-37 11 137 15 145
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
pfam00959 Phage_lysozyme 1.07e-15 30 133 3 107
Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDM07514.1 1.55e-104 1 144 1 144
QUU09268.1 1.55e-104 1 144 1 144
QDH56032.1 1.55e-104 1 144 1 144
QQA06365.1 1.55e-104 1 144 1 144
QUT29423.1 2.38e-99 1 144 1 144

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6ET6_A 5.03e-23 11 135 60 189
ChainA, Lysozyme [Acinetobacter baumannii]
6H9D_A 2.19e-17 11 132 14 139
ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
3HDF_A 5.46e-16 15 135 10 131
ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A 9.42e-16 15 135 35 156
ChainA, Lysozyme [Enterobacteria phage P21],3HDE_B Chain B, Lysozyme [Enterobacteria phage P21],3HDE_C Chain C, Lysozyme [Enterobacteria phage P21],3HDE_D Chain D, Lysozyme [Enterobacteria phage P21]
4ZPU_A 1.62e-15 15 135 35 156
Thestructure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_B The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_C The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_D The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9T1T5 1.94e-29 11 140 11 144
Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
P11187 2.31e-23 9 135 9 138
Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P07540 4.54e-23 9 135 9 138
Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
Q37896 4.97e-23 9 135 9 138
Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
O80292 9.60e-20 15 135 37 158
SAR-endolysin OS=Bacteriophage PS119 OX=83128 GN=19 PE=3 SV=1

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
0.829886 0.031337 0.137936 0.000139 0.000225 0.000476

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002549_01890.