Species | Rhizophagus irregularis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Mucoromycota; Glomeromycetes; ; Glomeraceae; Rhizophagus; Rhizophagus irregularis | |||||||||||
CAZyme ID | FUN_020455-T1-p1 | |||||||||||
CAZy Family | GT20 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA1 | 91 | 560 | 1e-113 | 0.9776536312849162 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
274555 | ascorbase | 1.24e-95 | 74 | 560 | 1 | 517 | L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases. |
215324 | PLN02604 | 1.61e-84 | 74 | 572 | 24 | 559 | oxidoreductase |
177843 | PLN02191 | 2.25e-80 | 87 | 566 | 36 | 546 | L-ascorbate oxidase |
225043 | SufI | 1.47e-66 | 89 | 568 | 48 | 450 | Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
274556 | laccase | 2.07e-65 | 74 | 577 | 3 | 530 | laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
6.27e-106 | 72 | 543 | 104 | 587 | |
9.43e-105 | 74 | 584 | 122 | 655 | |
2.16e-103 | 63 | 584 | 13 | 502 | |
1.50e-102 | 69 | 584 | 181 | 722 | |
3.47e-101 | 79 | 586 | 29 | 508 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.24e-95 | 72 | 584 | 4 | 485 | T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata] |
|
5.24e-95 | 79 | 584 | 8 | 485 | Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii] |
|
1.12e-93 | 79 | 584 | 8 | 485 | PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae] |
|
4.51e-93 | 79 | 584 | 8 | 486 | Laccase from Antrodiella faginea [Antrodiella faginea] |
|
6.16e-93 | 79 | 584 | 8 | 485 | Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_B Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1],5ANH_C Crystal Structure Of Laccase From Basidiomycete Pm1 (cect 2971) [basidiomycete PM1] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.35e-96 | 74 | 584 | 21 | 509 | Laccase-1 OS=Agaricus bisporus OX=5341 GN=lcc1 PE=1 SV=1 |
|
5.31e-94 | 74 | 584 | 21 | 509 | Laccase-2 OS=Agaricus bisporus OX=5341 GN=lcc2 PE=1 SV=1 |
|
1.13e-92 | 72 | 584 | 25 | 509 | Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2 |
|
2.69e-89 | 75 | 569 | 23 | 499 | Laccase-4 OS=Thanatephorus cucumeris OX=107832 GN=LCC4 PE=1 SV=1 |
|
1.17e-87 | 79 | 584 | 29 | 509 | Laccase OS=Trametes hirsuta OX=5327 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.001073 | 0.998879 | CS pos: 22-23. Pr: 0.9157 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.