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CAZyme Information: jhhlp_000612-t41_1-p1

You are here: Home > Sequence: jhhlp_000612-t41_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Lomentospora prolificans
Lineage Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
CAZyme ID jhhlp_000612-t41_1-p1
CAZy Family AA3
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
705 78091.51 5.2158
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_LprolificansJHH5317 8768 N/A 208 8560
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in jhhlp_000612-t41_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 144 668 1.4e-108 0.9776536312849162

CDD Domains      download full data without filtering help

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.

CAZyme Hits      help

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

PDB Hits      download full data without filtering help

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]
4.29e-65 120 678 16 508
Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits      download full data without filtering help

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
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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999777 0.000238

TMHMM  Annotations      download full data without filtering help

Start End
68 90