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CAZyme Information: MGYG000001027_01469

You are here: Home > Sequence: MGYG000001027_01469

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 CAG-56 sp900752065
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-56; CAG-56 sp900752065
CAZyme ID MGYG000001027_01469
CAZy Family GH24
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
180 20856.49 10.5575
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001027 2760146 MAG Sweden Europe
Gene Location Start: 957;  End: 1499  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001027_01469.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00737 lyz_endolysin_autolysin 4.55e-13 52 178 5 135
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.
cd16900 endolysin_R21-like 5.01e-07 52 173 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AII64150.1 9.35e-126 10 180 1 171
QUT30509.1 9.35e-126 10 180 1 171
QUT47425.1 9.35e-126 10 180 1 171
QUT63289.1 6.47e-125 11 180 17 186
QUT40153.1 2.47e-121 10 180 1 171

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.000506 0.998696 0.000214 0.000204 0.000168 0.000152

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001027_01469.