Species | Podospora comata | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora comata | |||||||||||
CAZyme ID | VBB75604.1 | |||||||||||
CAZy Family | AA9 | |||||||||||
CAZyme Description | Putative Glycoside Hydrolase Family 115 | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
EC | 3.2.1.131:6 |
---|
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH115 | 38 | 670 | 1.4e-217 | 0.8493543758967002 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
406396 | Glyco_hydro_115 | 5.06e-180 | 195 | 531 | 1 | 333 | Glycosyl hydrolase family 115. Glyco_hydro_115 is a family of glycoside hydrolases likely to have the activity of xylan a-1,2-glucuronidase, EC:3.2.1.131, or a-(4-O-methyl)-glucuronidase EC:3.2.1.-. |
407695 | GH115_C | 8.76e-63 | 800 | 970 | 1 | 172 | Gylcosyl hydrolase family 115 C-terminal domain. This domain is found at the C-terminus of glycosyl hydrolase family 115 proteins. This domain has a beta-sandwich fold. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 974 | 1 | 974 | |
0.0 | 1 | 974 | 1 | 955 | |
0.0 | 1 | 974 | 1 | 955 | |
9.10e-314 | 30 | 974 | 23 | 965 | |
1.47e-312 | 30 | 974 | 23 | 965 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.59e-171 | 29 | 971 | 7 | 933 | Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40],4ZMH_B Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40] |
|
5.31e-143 | 30 | 657 | 37 | 652 | Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C90_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_A Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus] |
|
4.70e-133 | 47 | 657 | 27 | 637 | Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
|
3.45e-132 | 47 | 657 | 26 | 636 | Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
|
7.90e-117 | 55 | 974 | 29 | 966 | Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112],6NPS_B Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112] |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000221 | 0.999729 | CS pos: 20-21. Pr: 0.9805 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.