Species | Magnaporthiopsis poae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae | |||||||||||
CAZyme ID | KLU82454.1 | |||||||||||
CAZy Family | AA7 | |||||||||||
CAZyme Description | GH131_N domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0C4DNX7] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH131 | 24 | 282 | 2.9e-76 | 0.9686274509803922 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
408085 | GH131_N | 1.08e-89 | 22 | 281 | 1 | 251 | Glycoside hydrolase 131 catalytic N-terminal domain. This is the N-terminal domain found in glycoside hydrolase family 131 (GH131A) protein observed in Coprinopsis cinerea. GH131A exhibits bifunctional exo-beta-1,3-/-1,6- and endo-beta-1,4 activity toward beta-glucan. This domain is catalytic in nature though the catalytic mechanism of C. cinerea GH131A is different from that of typical glycosidases that use a pair of carboxylic acid residues as the catalytic residues. In the case of GH131A, Glu98 and His218 may form a catalytic dyad and Glu98 may activate His218 during catalysis. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
3.54e-134 | 15 | 289 | 20 | 296 | |
5.73e-122 | 12 | 287 | 90 | 365 | |
3.43e-114 | 9 | 287 | 10 | 285 | |
2.41e-107 | 14 | 287 | 16 | 276 | |
5.05e-103 | 4 | 286 | 8 | 277 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.557722 | 0.442273 |
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