Species | Trichosporon asahii | |||||||||||
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Lineage | Basidiomycota; Tremellomycetes; ; Trichosporonaceae; Trichosporon; Trichosporon asahii | |||||||||||
CAZyme ID | EJT45968.1 | |||||||||||
CAZy Family | AA2 | |||||||||||
CAZyme Description | GH16 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:J5Q819] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH16 | 119 | 357 | 9.5e-62 | 0.9781659388646288 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
185690 | GH16_fungal_Lam16A_glucanase | 1.36e-97 | 80 | 380 | 6 | 293 | fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Group of fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Lam16A belongs to the 'nonspecific' 1,3(4)-beta-glucanase subfamily, although beta-1,6 branching and beta-1,4 bonds specifically define where Lam16A hydrolyzes its substrates, like curdlan (beta-1,3-glucan), lichenin (beta-1,3-1,4-mixed linkage glucan), and laminarin (beta-1,6-branched-1,3-glucan). |
185693 | GH16_laminarinase_like | 1.94e-12 | 165 | 210 | 88 | 135 | Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans. |
185691 | GH16_Strep_laminarinase_like | 1.53e-08 | 168 | 229 | 104 | 173 | Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel. |
225182 | BglS | 0.001 | 165 | 216 | 127 | 178 | Beta-glucanase, GH16 family [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.37e-61 | 76 | 379 | 139 | 446 | |
4.13e-60 | 83 | 379 | 27 | 312 | |
5.83e-60 | 16 | 379 | 57 | 424 | |
2.73e-59 | 16 | 379 | 79 | 446 | |
2.73e-59 | 16 | 379 | 79 | 446 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.97e-59 | 84 | 379 | 11 | 295 | The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_B The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_C The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'],3WDU_D The complex structure of PtLic16A with cellobiose [Paecilomyces sp. 'thermophila'] |
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3.06e-59 | 84 | 379 | 12 | 296 | The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_B The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_C The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDT_D The apo-form structure of PtLic16A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDV_A The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_B The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_C The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDV_D The complex structure of PtLic16A with cellotetraose [Paecilomyces sp. 'thermophila'] |
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2.25e-58 | 84 | 379 | 10 | 294 | The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_B The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_C The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'],3WDY_D The complex structure of E113A with cellotetraose [Paecilomyces sp. 'thermophila'] |
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2.39e-58 | 84 | 379 | 12 | 296 | The apo-form structure of E113A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDW_B The apo-form structure of E113A from Paecilomyces thermophila [Paecilomyces sp. 'thermophila'],3WDX_A The complex structure of E113A with glucotriose [Paecilomyces sp. 'thermophila'],3WDX_B The complex structure of E113A with glucotriose [Paecilomyces sp. 'thermophila'] |
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6.67e-58 | 81 | 380 | 8 | 298 | Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase [Paecilomyces sp. 'thermophila'],5JVV_B Crystal structure and characterization an elongating GH family 16 beta-1,3-glucosyltransferase [Paecilomyces sp. 'thermophila'] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.93e-55 | 82 | 381 | 26 | 316 | Endo-1,3(4)-beta-glucanase ARB_04519 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_04519 PE=3 SV=1 |
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2.23e-55 | 80 | 379 | 133 | 417 | Probable glycosidase C21B10.07 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPBC21B10.07 PE=3 SV=1 |
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3.30e-55 | 80 | 379 | 36 | 326 | Probable endo-1,3(4)-beta-glucanase NFIA_089530 OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=NFIA_089530 PE=3 SV=1 |
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2.40e-54 | 80 | 379 | 36 | 326 | Probable endo-1,3(4)-beta-glucanase AFUB_029980 OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=AFUB_029980 PE=3 SV=1 |
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2.40e-54 | 80 | 379 | 36 | 326 | Probable endo-1,3(4)-beta-glucanase AFUA_2G14360 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=AFUA_2G14360 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000303 | 0.999663 | CS pos: 20-21. Pr: 0.9699 |
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