Species | Enterococcus_B faecium | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_B; Enterococcus_B faecium | |||||||||||
CAZyme ID | MGYG000002353_01159 | |||||||||||
CAZy Family | GH23 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1173791; End: 1174429 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK11198 | PRK11198 | 4.88e-12 | 23 | 77 | 90 | 146 | LysM domain/BON superfamily protein; Provisional |
pfam01476 | LysM | 1.57e-10 | 31 | 77 | 1 | 43 | LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known. |
cd00118 | LysM | 4.66e-10 | 31 | 76 | 3 | 45 | Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes. |
smart00257 | LysM | 8.03e-10 | 31 | 76 | 2 | 44 | Lysin motif. |
COG1652 | XkdP | 4.30e-04 | 14 | 81 | 196 | 266 | Nucleoid-associated protein YgaU, contains BON and LysM domains [Function unknown]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QHU87361.1 | 1.58e-128 | 1 | 212 | 1 | 212 |
APJ06472.1 | 1.58e-128 | 1 | 212 | 1 | 212 |
ATW36015.1 | 1.58e-128 | 1 | 212 | 1 | 212 |
QCV52479.1 | 1.58e-128 | 1 | 212 | 1 | 212 |
AOM15727.1 | 1.58e-128 | 1 | 212 | 1 | 212 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5FIM_A | 3.50e-06 | 23 | 79 | 91 | 149 | Thestructure of Kbp.K from E. coli [Escherichia coli],7PVC_A Chain A, Potassium binding protein Kbp [Escherichia coli K-12] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000481 | 0.998601 | 0.000214 | 0.000255 | 0.000224 | 0.000194 |
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