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CAZyme Information: QYA_142925T0-p1

You are here: Home > Sequence: QYA_142925T0-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 Mucor lusitanicus
Lineage Mucoromycota; Mucoromycetes; ; Mucoraceae; Mucor; Mucor lusitanicus
CAZyme ID QYA_142925T0-p1
CAZy Family GH29
CAZyme Description Multicopper oxidase [Source:UniProtKB/TrEMBL;Acc:A0A168L023]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
556 63478.30 7.3807
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MlusitanicusCBS277-49 11852 747725 0 11852
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in QYA_142925T0-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 44 536 8.4e-95 0.9664804469273743

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
274555 ascorbase 4.61e-91 24 550 3 530
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.
177843 PLN02191 3.32e-87 7 550 8 553
L-ascorbate oxidase
215324 PLN02604 2.62e-78 1 550 2 553
oxidoreductase
132431 ascorbOXfungal 3.00e-71 47 536 31 524
L-ascorbate oxidase, fungal type. This model describes a family of fungal ascorbate oxidases, within a larger family of multicopper oxidases that also includes plant ascorbate oxidases (TIGR03388), plant laccases and laccase-like proteins (TIGR03389), and related proteins. The member from Acremonium sp. HI-25 is characterized.
274556 laccase 2.84e-65 20 541 1 518
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
8.10e-165 25 555 28 652
5.86e-145 25 548 30 573
5.57e-141 25 548 18 570
2.31e-114 7 515 4 519
9.27e-74 11 550 8 549

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.02e-68 20 548 1 528
Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1AOZ_B Refined Crystal Structure Of Ascorbate Oxidase At 1.9 Angstroms Resolution [Cucurbita pepo var. melopepo],1ASO_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASO_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASP_A X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASP_B X-ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-forms [Cucurbita pepo var. melopepo],1ASQ_A X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo],1ASQ_B X-Ray Structures And Mechanistic Implications Of Three Functional Derivatives Of Ascorbate Oxidase From Zucchini: Reduced-, Peroxide-, And Azide-Forms [Cucurbita pepo var. melopepo]
3.18e-55 49 549 28 485
Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
6.83e-47 26 547 7 474
Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
9.43e-47 26 547 7 474
Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta]
1.80e-46 26 547 7 474
Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.52e-72 20 550 18 549
L-ascorbate oxidase OS=Brassica rapa subsp. pekinensis OX=51351 GN=AO PE=2 SV=1
3.69e-72 15 548 28 564
L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
3.36e-69 20 550 28 557
L-ascorbate oxidase OS=Nicotiana tabacum OX=4097 GN=AAO PE=2 SV=1
1.04e-67 20 548 1 528
L-ascorbate oxidase OS=Cucurbita pepo var. melopepo OX=3665 PE=1 SV=1
1.64e-67 36 550 37 550
L-ascorbate oxidase OS=Arabidopsis thaliana OX=3702 GN=AAO PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000239 0.999743 CS pos: 20-21. Pr: 0.9799

TMHMM  Annotations      help

There is no transmembrane helices in QYA_142925T0-p1.