Species | Cryptococcus neoformans | |||||||||||
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Lineage | Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus neoformans | |||||||||||
CAZyme ID | CNBI0610-t26_1-p1 | |||||||||||
CAZy Family | GT1 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.131:6 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH115 | 87 | 717 | 3.9e-241 | 0.8378766140602583 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
406396 | Glyco_hydro_115 | 1.65e-165 | 234 | 586 | 1 | 334 | 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 | 1.69e-59 | 880 | 1073 | 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. |
271342 | BACON | 0.010 | 797 | 866 | 25 | 80 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 1077 | 1 | 1076 | |
0.0 | 1 | 1077 | 1 | 1076 | |
0.0 | 1 | 1077 | 1 | 1086 | |
0.0 | 204 | 1077 | 1 | 874 | |
0.0 | 1 | 1068 | 1 | 992 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.27e-180 | 107 | 1076 | 38 | 935 | 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] |
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1.74e-125 | 102 | 755 | 63 | 694 | 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] |
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1.96e-119 | 102 | 755 | 36 | 679 | Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
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1.03e-116 | 102 | 755 | 35 | 678 | Chain A, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
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2.51e-113 | 108 | 1077 | 36 | 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 |
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0.000250 | 0.999743 | CS pos: 23-24. Pr: 0.9796 |
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