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CAZyme Information: MGYG000000245_03423

You are here: Home > Sequence: MGYG000000245_03423

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 Roseburia sp003470905
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia sp003470905
CAZyme ID MGYG000000245_03423
CAZy Family GH24
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
224 24505.08 10.027
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000245 4145433 Isolate China Asia
Gene Location Start: 21841;  End: 22515  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000245_03423.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH24 6 137 5.8e-42 0.9927007299270073

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00737 lyz_endolysin_autolysin 1.46e-63 10 142 1 136
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 8.38e-43 6 140 2 138
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 2.86e-39 6 141 7 147
Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16900 endolysin_R21-like 3.60e-30 9 140 7 140
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.
cd00735 T4-like_lys 5.75e-16 12 136 4 137
bacteriophage T4-like lysozymes. Bacteriophage T4-like lysozymes hydrolyze the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in peptidoglycan heteropolymers of prokaryotic cell walls. Members include a variety of bacteriophages (T4, RB49, RB69, Aeh1), as well as Dictyostelium.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VCV22350.1 2.32e-125 1 224 1 226
VUE37339.1 2.32e-125 1 224 1 226
QLG39410.1 1.29e-47 4 159 2 154
QYK68242.1 7.12e-47 4 147 2 148
QDY81941.1 7.61e-46 4 143 2 144

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6ET6_A 4.15e-25 10 144 56 196
ChainA, Lysozyme [Acinetobacter baumannii]
6H9D_A 5.84e-23 2 141 2 146
ChainA, Lysozyme [Asticcacaulis excentricus],6H9D_B Chain B, Lysozyme [Asticcacaulis excentricus],6H9D_C Chain C, Lysozyme [Asticcacaulis excentricus]
7M5I_A 2.87e-17 5 141 8 153
ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
2ANV_A 2.31e-14 5 141 3 144
ChainA, Lysozyme [Lederbergvirus P22],2ANV_B Chain B, Lysozyme [Lederbergvirus P22],2ANX_A Chain A, Lysozyme [Lederbergvirus P22],2ANX_B Chain B, Lysozyme [Lederbergvirus P22]
1XJU_A 6.44e-13 5 101 1 94
ChainA, Lysozyme [Punavirus P1],1XJU_B Chain B, Lysozyme [Punavirus P1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9T1T5 5.24e-27 6 141 3 143
Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
P62692 7.02e-22 5 145 2 140
Endolysin OS=Lactococcus phage c2 OX=31537 GN=L3 PE=3 SV=1
P62693 7.02e-22 5 145 2 140
Endolysin OS=Lactococcus phage phivML3 OX=10746 GN=L3 PE=3 SV=1
P11187 1.89e-17 5 164 2 167
Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
P07540 2.62e-17 5 142 2 143
Endolysin OS=Bacillus phage PZA OX=10757 GN=15 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
1.000043 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000245_03423.