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CAZyme Information: MGYG000000124_01480

You are here: Home > Sequence: MGYG000000124_01480

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 Citrobacter youngae
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter; Citrobacter youngae
CAZyme ID MGYG000000124_01480
CAZy Family GH24
CAZyme Description Lysozyme RrrD
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
179 19458.39 9.093
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000124 5038075 Isolate Canada North America
Gene Location Start: 1501653;  End: 1502192  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.17

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH24 27 169 2.5e-39 0.9562043795620438

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3772 RrrD 1.19e-56 16 178 1 152
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900 endolysin_R21-like 2.69e-56 19 174 1 142
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 1.32e-28 48 167 2 107
Phage lysozyme. This family includes lambda phage lysozyme and E. coli endolysin.
cd00737 lyz_endolysin_autolysin 1.47e-26 28 147 3 119
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 1.22e-15 34 172 14 138
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VEI41613.1 1.40e-133 1 179 1 179
ALD75810.1 3.04e-128 1 179 1 179
QPO98300.1 4.32e-128 1 179 1 179
AXZ48583.1 1.38e-127 5 179 8 182
AXL99234.1 5.05e-127 1 179 1 179

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7M5I_A 1.78e-22 34 172 21 152
ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
3HDE_A 2.62e-19 3 176 4 163
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 6.47e-19 3 176 4 163
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]
3HDF_A 1.12e-18 31 176 7 138
ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
6ET6_A 8.64e-15 28 172 58 192
ChainA, Lysozyme [Acinetobacter baumannii]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O64362 1.13e-117 3 179 2 178
SAR-endolysin OS=Escherichia phage N15 OX=40631 GN=54 PE=3 SV=1
P68921 2.54e-107 8 179 9 177
SAR-endolysin OS=Enterobacteria phage VT2-Sa OX=97081 GN=R PE=3 SV=1
P68920 2.54e-107 8 179 9 177
SAR-endolysin OS=Escherichia phage 933W OX=10730 GN=R PE=3 SV=1
Q9ZXB7 9.89e-105 8 179 9 177
SAR-endolysin OS=Enterobacteria phage H19B OX=69932 GN=R PE=3 SV=1
P76159 8.12e-104 8 179 9 177
Probable prophage lysozyme OS=Escherichia coli (strain K12) OX=83333 GN=rrrQ PE=3 SV=1

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
0.107526 0.890963 0.000656 0.000294 0.000260 0.000270

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000124_01480.