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CAZyme Information: MGYG000002668_02035

You are here: Home > Sequence: MGYG000002668_02035

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 Prevotella sp900552965
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900552965
CAZyme ID MGYG000002668_02035
CAZy Family GH24
CAZyme Description Lysozyme RrrD
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
134 15244.57 9.5792
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002668 2820424 MAG United Republic of Tanzania Africa
Gene Location Start: 38;  End: 442  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002668_02035.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH24 1 126 6.7e-46 0.9416058394160584

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00737 lyz_endolysin_autolysin 1.12e-71 1 131 4 136
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 2.12e-52 1 129 9 138
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.
COG3772 RrrD 4.36e-46 2 134 15 151
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900 endolysin_R21-like 3.46e-44 1 129 11 140
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.
pfam00959 Phage_lysozyme 6.25e-22 19 123 1 106
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
QUT29423.1 6.70e-46 2 130 11 139
QDM07514.1 2.21e-44 2 130 11 139
QUU09268.1 2.21e-44 2 130 11 139
QDH56032.1 2.21e-44 2 130 11 139
QQA06365.1 2.21e-44 2 130 11 139

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6ET6_A 3.75e-29 1 132 59 195
ChainA, Lysozyme [Acinetobacter baumannii]
6H9D_A 7.26e-25 1 132 13 148
ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
3HDF_A 2.08e-19 6 129 10 134
ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
3HDE_A 3.76e-19 6 129 35 159
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 9.30e-19 6 129 35 159
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 1.47e-31 1 132 10 145
Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
P07540 1.99e-25 1 132 10 144
Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
P11187 7.74e-25 1 132 10 144
Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
Q37896 5.28e-22 1 134 10 146
Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
O80292 8.81e-21 6 126 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
1.000047 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002668_02035.