Species | Magnaporthiopsis poae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae | |||||||||||
CAZyme ID | KLU82997.1 | |||||||||||
CAZy Family | AA9 | |||||||||||
CAZyme Description | GH131_N domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0C4DQC5] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH131 | 39 | 302 | 7.2e-69 | 0.9647058823529412 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
408085 | GH131_N | 1.86e-64 | 39 | 302 | 3 | 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 |
---|---|---|---|---|---|
3.85e-157 | 1 | 306 | 4 | 302 | |
2.05e-64 | 31 | 306 | 29 | 303 | |
1.09e-55 | 37 | 306 | 31 | 299 | |
5.54e-53 | 39 | 306 | 32 | 292 | |
4.95e-51 | 26 | 306 | 24 | 294 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000398 | 0.999584 | CS pos: 29-30. Pr: 0.9543 |
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