Species | Lomentospora prolificans | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans | |||||||||||
CAZyme ID | jhhlp_000612-t41_1-p1 | |||||||||||
CAZy Family | AA3 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA1 | 144 | 668 | 1.4e-108 | 0.9776536312849162 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
274555 | ascorbase | 4.64e-69 | 127 | 681 | 1 | 530 | 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. |
259926 | CuRO_1_Diphenol_Ox | 1.77e-64 | 128 | 247 | 1 | 119 | The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. |
225043 | SufI | 1.45e-61 | 151 | 668 | 57 | 442 | 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]. |
177843 | PLN02191 | 2.65e-61 | 128 | 699 | 24 | 567 | L-ascorbate oxidase |
274556 | laccase | 6.56e-60 | 127 | 671 | 3 | 516 | 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 |
---|---|---|---|---|---|
3.35e-204 | 93 | 700 | 89 | 688 | |
6.63e-167 | 104 | 687 | 93 | 669 | |
2.22e-156 | 107 | 701 | 117 | 692 | |
2.22e-156 | 107 | 701 | 117 | 692 | |
4.36e-153 | 107 | 701 | 117 | 692 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.22e-69 | 112 | 689 | 51 | 555 | Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada] |
|
3.27e-69 | 112 | 689 | 51 | 555 | Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada] |
|
2.58e-66 | 134 | 674 | 10 | 468 | Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus] |
|
4.14e-66 | 101 | 678 | 23 | 536 | Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger] |
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4.29e-65 | 120 | 678 | 16 | 508 | Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.79e-90 | 115 | 667 | 49 | 553 | Laccase-1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC1 PE=1 SV=1 |
|
5.71e-89 | 115 | 672 | 49 | 558 | Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1 |
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8.80e-85 | 115 | 674 | 49 | 561 | Laccase-2 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=LAC2 PE=3 SV=2 |
|
1.82e-71 | 134 | 670 | 33 | 493 | Laccase-5 OS=Trametes villosa OX=47662 GN=LCC5 PE=3 SV=2 |
|
9.54e-71 | 134 | 674 | 33 | 497 | Laccase-5 OS=Trametes versicolor OX=5325 GN=LCC5 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.999777 | 0.000238 |
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