Species | Prevotella bivia | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella bivia | |||||||||||
CAZyme ID | MGYG000003374_01154 | |||||||||||
CAZy Family | GH24 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1765; End: 2271 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00737 | lyz_endolysin_autolysin | 3.48e-12 | 41 | 135 | 5 | 104 | 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. |
cd00735 | T4-like_lys | 0.002 | 42 | 133 | 7 | 111 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ATV27155.1 | 2.44e-115 | 1 | 168 | 1 | 168 |
QUB50441.1 | 2.63e-110 | 1 | 168 | 1 | 168 |
AWX07865.1 | 2.16e-109 | 1 | 168 | 1 | 168 |
QUB50449.1 | 8.80e-109 | 1 | 168 | 1 | 168 |
QUB89297.1 | 1.46e-107 | 1 | 167 | 1 | 167 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000236 | 0.999186 | 0.000193 | 0.000140 | 0.000126 | 0.000122 |
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