CAZyme Information: AYO41925.1

Basic Information

• Species: Malassezia restricta
• Lineage: Basidiomycota; Malasseziomycetes; ; Malasseziaceae; Malassezia; Malassezia restricta
• CAZyme ID: AYO41925.1
• CAZy Family: GH16
• CAZyme Description: Laccase-5

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
681		77453.36	6.7580

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MrestrictaCBS7877	4155	425264	59	4096

• Gene Location: location=CP033149:387378-389423(-)

Full Sequence      

MVASKQPWGLRQWMLLVIGAGLLGLFSCLIWTDVALQQSLLHTWDQGWQVVRKQSMAYYQ
QSPVSMNTKFNTSESPRERVFDWTVDRRIQAPDGVPRLMYTINGQFPGPTIQATVGDTVV
VHVRNRINDDYVVPDPPTTSKLESVHPKGTDRKFSLHWHGLSMRGSDEMDGAAAFTSCPL
QPGNETTYRFVVHQEDVGTHWYHSHVGTSRADGLWGMLIVHAREDERKVLKERAPTFDTH
WDEEIPIALGDHFHKMSPESLAKYVSIVLGEAEPVPESGLINGRHIFSCDMARYTGVPCP
AGDKDEVGEYTEFHLRHDKQYRLRLVNVGSIADITFSVDGHTMTVIEADGTLVEPMHVHR
IPISPGQRYSVILHREPSMKDSRVWMRAELQGECFKYMNPVLDPFIKAIVVYDNASPKDD
WLAPLRVRQNYAKRFGPFRAFAKSERPTTHPWSPDIQDQGIPTEPCHDLEPGTLVPLIPD
PAPEFHPERGDRREIINIEVLIRQKFRAPMSYMNLSSWRPYGARGPAMQPLLHRISHSNL
TTAEEWEAHGLVNREHELVVSTHPTKPIVYDLVIVNLDDGPHPFHLHGHKFWVLHTGEME
VPSYRYKPEVEKEFDLKRAMKRDTVVVPMMGHAIIRWVADNPGVWAFHCHMLVHLASGMA
MAIVEQPALLQANPSVPSTCQ

Enzyme Prediction     

No EC number prediction in AYO41925.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	95	660	1.3e-98	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	6.18e-83	79	665	2	523	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	1.70e-76	73	665	18	546	L-ascorbate oxidase
259953	CuRO_2_MCO_like_1	8.88e-71	247	413	3	163	The second 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 oxidise 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 family of MCOs is composed of three cupredoxin domains 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 2 of 3-domain MCOs has lost the ability to bind copper.
259977	CuRO_3_MCO_like_4	1.06e-56	502	665	9	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	6.10e-56	77	665	23	546	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYO41925.1|AA1	0.0	1	681	1	681
AXA49146.1|AA1	0.0	1	681	1	681
AYO41924.1|AA1	8.20e-318	63	681	69	696
AXA49143.1|AA1	8.20e-318	63	681	69	696
CBQ71635.1|AA1	4.77e-124	75	676	58	633

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	7.20e-60	79	680	4	538	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]
5LM8_A	2.09e-50	77	666	24	505	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.12e-50	77	666	25	506	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
1ZPU_A	2.19e-50	81	671	5	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]
5LWX_A	3.35e-50	77	666	52	533	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8LPL3|ASO_ARATH	2.44e-67	83	665	28	543	L-ascorbate oxidase OS=Arabidopsis thaliana OX=3702 GN=AAO PE=1 SV=1
sp|Q40588|ASO_TOBAC	7.07e-64	77	680	29	565	L-ascorbate oxidase OS=Nicotiana tabacum OX=4097 GN=AAO PE=2 SV=1
sp|P14133|ASO_CUCSA	3.14e-63	76	680	36	574	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	8.98e-63	62	670	45	565	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
sp|Q55P57|LAC1_CRYNB	6.28e-62	62	670	45	565	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.987360	0.012673

TMHMM  Annotations     

Start	End
13	35