CAZyme Information: SHO80146.1

Basic Information

• Species: Malassezia sympodialis
• Lineage: Basidiomycota; Malasseziomycetes; ; Malasseziaceae; Malassezia; Malassezia sympodialis
• CAZyme ID: SHO80146.1
• CAZy Family: GT59
• CAZyme Description: Similar to S.cerevisiae protein FET5 (Multicopper oxidase) [Source:UniProtKB/TrEMBL;Acc:A0A1M8ACE6]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
695	LT671828|CGC2	78795.31	6.4332

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MsympodialisATCC42132	4618	1230383	143	4475

• Gene Location: location=LT671828:415724-417811(+)

Full Sequence      

MMSLRPKAWRIAPSLLLLVTSVLLAMYVWLNHTDALVAQSLGRLWNIGFQNPLSTIDAFA
TDRVTTGPLAMDPSYNSTELPRERVFDWTVERAEQSPDGIPRLMYTINGQFPGPIIEATE
GDTVVVRVRNHIYDNFTIPPPPLSSQRDDVHPDGTDRKFTFHWHGLSMRNTQVMDGASAF
TSCALLPGEEREYRFLVHPEDVGTHWYHSHVGTSRADGLWGMFIVHSRTDERKKLSTRFP
DANTHWNEEVAIALGDHYHQFGPISLGFYVSRWLQKAEPVPENALINGKHVFSCHHSRLT
GVPCPAGDVDQVGEYSTFSLDPKQAYRLRLVNVGALADITFSVDGHTMTVIEADGTLVEP
VRVHRIPIAPGQRYSVILHREPKSKDSRVWMRADMSAECFQYTNPVMELGAKAIIAYDTR
QSGEESKDDWKSLLRLRSYKRGLTDRIWHGSWFQSQLPATLPWNPNVTDTILPEEPCHDL
EPDTLVPLIPDPAPPLRLDQGDHREFVFVTAPILERYGVVPMGFMNGSTWRPYGRHGRER
QPLLHRISYANTSTVQGWHDQDILDPSHELVASPHPSRPVVMEMVINNQDDSPHPFHLHG
HKFWVMETGEADPNFGGFDYYEDVGQVYNLNRKMKRDTVIVPMMGHAVIRWVADNPGVWA
FHCHMLVHLASGMAMAIVEQPEVLQAQPPVQRTCS

Enzyme Prediction     

No EC number prediction in SHO80146.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	100	674	1.6e-94	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.74e-70	84	679	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.
259953	CuRO_2_MCO_like_1	3.20e-69	250	418	1	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.
177843	PLN02191	6.73e-65	84	679	24	546	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	4.60e-59	506	679	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	4.52e-56	82	694	23	561	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYO41924.1|AA1	0.0	14	694	13	695
AXA49143.1|AA1	0.0	14	694	13	695
AYO41925.1|AA1	6.38e-302	7	694	6	680
AXA49146.1|AA1	1.28e-301	7	694	6	680
CBQ71635.1|AA1	3.14e-136	74	691	52	634

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	1.28e-53	84	694	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]
3V9E_A	1.46e-46	50	679	33	542	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
1HFU_A	2.69e-46	89	691	10	482	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.74e-46	89	691	10	482	Chain A, Laccase [Coprinopsis cinerea]
1KYA_A	3.43e-46	85	691	5	482	Chain A, Laccase [Trametes versicolor],1KYA_B Chain B, Laccase [Trametes versicolor],1KYA_C Chain C, Laccase [Trametes versicolor],1KYA_D Chain D, Laccase [Trametes versicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VQZ4|LAC2_CRYNH	5.83e-60	65	685	41	566	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
sp|Q55P57|LAC1_CRYNB	6.64e-58	50	684	25	565	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|P14133|ASO_CUCSA	3.22e-57	80	694	35	574	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	2.09e-55	50	681	25	562	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|Q8LPL3|ASO_ARATH	3.97e-54	88	679	28	543	L-ascorbate oxidase OS=Arabidopsis thaliana OX=3702 GN=AAO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999559	0.000467

TMHMM  Annotations     

Start	End
13	30