Species | Pyricularia oryzae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Pyriculariaceae; Pyricularia; Pyricularia oryzae | |||||||||||
CAZyme ID | mRNA_M_BR32_EuGene_00085881-p1 | |||||||||||
CAZy Family | GT69 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
EC | 3.2.1.21:5 | 3.2.1.38:1 | 3.2.1.-:1 |
---|
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
224389 | BglX | 2.08e-25 | 54 | 409 | 1 | 363 | Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism]. |
185053 | PRK15098 | 5.38e-16 | 164 | 556 | 191 | 648 | beta-glucosidase BglX. |
395747 | Glyco_hydro_3 | 1.66e-15 | 55 | 342 | 1 | 315 | Glycosyl hydrolase family 3 N terminal domain. |
396478 | Glyco_hydro_3_C | 5.12e-05 | 421 | 556 | 84 | 216 | Glycosyl hydrolase family 3 C-terminal domain. This domain is involved in catalysis and may be involved in binding beta-glucan. This domain is found associated with pfam00933. |
235417 | PRK05337 | 4.67e-04 | 146 | 269 | 132 | 249 | beta-hexosaminidase; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 561 | 7 | 630 | |
2.07e-260 | 1 | 556 | 8 | 619 | |
2.77e-252 | 2 | 561 | 11 | 636 | |
2.19e-239 | 25 | 559 | 40 | 637 | |
5.51e-232 | 24 | 560 | 30 | 627 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.68e-21 | 34 | 557 | 38 | 615 | Crystal structure Glucan 1,4-beta-glucosidase from Saccharopolyspora erythraea [Saccharopolyspora erythraea D] |
|
3.94e-19 | 32 | 554 | 5 | 601 | Crystal structure of barley exohydrolaseI W434A mutant in complex with methyl 2-thio-beta-sophoroside. [Hordeum vulgare subsp. vulgare],6K6V_A Crystal structure of barley exohydrolaseI W434A mutant in complex with methyl 6-thio-beta-gentiobioside [Hordeum vulgare subsp. vulgare],6KUF_A Crystal structure of barley exohydrolaseI W434A mutant in complex with glucose. [Hordeum vulgare subsp. vulgare],6L1J_A Crystal structure of barley exohydrolaseI W434A mutant in complex with 4'-nitrophenyl thiolaminaritrioside [Hordeum vulgare subsp. vulgare],6LBB_A Crystal structure of barley exohydrolaseI W434A mutant in complex with 4I,4III,4V-S-trithiocellohexaose [Hordeum vulgare subsp. vulgare] |
|
5.14e-19 | 32 | 554 | 1 | 597 | Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with gluco-phenylimidazole [Hordeum vulgare],1X38_A crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with gluco-phenylimidazole [Hordeum vulgare],1X39_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with gluco-phenylimidazole [Hordeum vulgare] |
|
5.18e-19 | 32 | 554 | 1 | 597 | Beta-d-glucan Exohydrolase From Barley [Hordeum vulgare],1IEQ_A Crystal Structure Of Barley Beta-D-Glucan Glucohydrolase Isoenzyme Exo1 [Hordeum vulgare],1IEV_A Crystal Structure Of Barley Beta-d-glucan Glucohydrolase Isoenzyme Exo1 In Complex With Cyclohexitol [Hordeum vulgare],1IEW_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 2-deoxy-2-fluoro-alpha-D-glucoside [Hordeum vulgare],1IEX_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4I,4III,4V-S-trithiocellohexaose [Hordeum vulgare],1J8V_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme Exo1 in complex with 4'-nitrophenyl 3I-thiolaminaritrioside [Hordeum vulgare],3WLH_A Crystal Structure Analysis of Plant Exohydrolase [Hordeum vulgare subsp. vulgare],3WLJ_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme EXO1 in complex with 3-deoxy-glucose [Hordeum vulgare subsp. vulgare],3WLK_X Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme EXO1 in complex with 4-deoxy-glucose [Hordeum vulgare subsp. vulgare],3WLL_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme EXO1 in complex with PEG400 [Hordeum vulgare subsp. vulgare],3WLM_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme exo1 in complex with octyl-O-glucoside [Hordeum vulgare subsp. vulgare],3WLN_A Crystal structure of barley beta-D-glucan glucohydrolase isoenzyme EXO1 in complex with octyl-S-glucoside [Hordeum vulgare subsp. vulgare],3WLP_A Crystal Structure Analysis of Plant Exohydrolase [Hordeum vulgare subsp. vulgare] |
|
5.23e-19 | 32 | 554 | 5 | 601 | Crystal structure of barley exohydrolaseI W434H mutant in complex with methyl 2-thio-beta-sophoroside [Hordeum vulgare subsp. vulgare],6JGN_A Crystal structure of barley exohydrolaseI W434H in complex with 4'-nitrophenyl thiolaminaribioside [Hordeum vulgare subsp. vulgare],6JGO_A Crystal structure of barley exohydrolaseI W434H mutant in complex with 4I,4III,4V-S-trithiocellohexaose [Hordeum vulgare subsp. vulgare],6JGP_A Crystal structure of barley exohydrolaseI W434H mutant in complex with methyl 6-thio-beta-gentiobioside. [Hordeum vulgare subsp. vulgare] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.79e-233 | 24 | 560 | 30 | 627 | Probable beta-glucosidase C OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=bglC PE=3 SV=1 |
|
6.03e-230 | 24 | 560 | 34 | 631 | Probable beta-glucosidase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=bglC PE=3 SV=2 |
|
2.31e-217 | 33 | 556 | 35 | 615 | Beta-glucosidase C OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=bglC PE=1 SV=1 |
|
7.60e-77 | 21 | 556 | 39 | 654 | Periplasmic beta-glucosidase/beta-xylosidase OS=Dickeya chrysanthemi OX=556 GN=bgxA PE=3 SV=1 |
|
5.51e-23 | 20 | 558 | 16 | 640 | Putative beta-xylosidase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22230 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.820048 | 0.179981 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.