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CAZyme Information: KAB8202001.1

You are here: Home > Sequence: KAB8202001.1

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 Aspergillus parasiticus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus parasiticus
CAZyme ID KAB8202001.1
CAZy Family AA8|AA3
CAZyme Description multicopper oxidase-domain-containing protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
621 ML735010|CGC1 69314.33 6.3823
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AparasiticusCBS117618 14005 N/A 253 13752
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in KAB8202001.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA1 126 610 5.1e-90 0.9804469273743017

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
274555 ascorbase 3.43e-75 109 609 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.
177843 PLN02191 7.23e-68 114 612 28 543
L-ascorbate oxidase
225043 SufI 6.33e-67 114 618 38 451
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].
259977 CuRO_3_MCO_like_4 4.70e-61 456 615 2 166
The third cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
215324 PLN02604 4.32e-60 109 616 24 547
oxidoreductase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 620 1 620
0.0 1 620 1 620
0.0 18 620 1 603
0.0 176 620 1 445
2.76e-248 38 615 13 586

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.06e-58 109 613 2 477
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]
3.20e-57 110 616 4 524
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]
7.69e-51 108 611 66 538
Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
2.00e-50 108 611 66 538
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]
6.01e-45 106 613 3 465
Laccase from Antrodiella faginea [Antrodiella faginea]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.63e-65 57 615 5 560
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
5.45e-64 107 615 59 560
Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
4.18e-63 107 615 59 560
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
1.10e-59 109 613 27 503
Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
2.49e-59 114 616 25 543
L-ascorbate oxidase OS=Brassica rapa subsp. pekinensis OX=51351 GN=AO PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999964 0.000038

TMHMM  Annotations      download full data without filtering help

Start End
36 58