CAZyme Information: MGL_3079-t26_1-p1

Basic Information

• Species: Malassezia globosa
• Lineage: Basidiomycota; Malasseziomycetes; ; Malasseziaceae; Malassezia; Malassezia globosa
• CAZyme ID: MGL_3079-t26_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
655	AAYY01000011|CGC3	74621.81	6.5686

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MglobosaCBS7966	4286	425265	0	4286

• Gene Location: location=AAYY01000011:15433-17400(-)

Full Sequence      

MDVTLQQTLQHAWDESWSALRVYTALKQQSDPMALDASFNPNEAPRERVYDWTVDRRIQA
PDGVPRLMYTINGKFPGPTIQATVGDTVVVHVRNHIWDDYQVPEPPITSKLDHVHPEGTD
RKFAIHWHGLSMRGTQVMDGAAAFTSCPLKPGNETTYRFVVHPEDVGTHWYHSHVGTSRA
DGLWGMLIVHAREDERKVLKERAPAHETHWDEEVAIAVGDHFHEMSPQSLGKYVSIILSS
AEPVPDSGLINGKHIFSCNMSRITDVPCPAGDKDEVGEYAQFHLRHDQQYRLRLVNVGSL
ADVMFSVDEHTMTVIEADGVLVEPMKVHRIPISPGQRYSVILHREPSSKRHERVWMRAEL
EGECFKYMNPVLDPFLKAIVTYDVNMPPLSGGWLSPLRARQLFGQQATEKHRRYTSASKR
PTTQAWSPDIKDEGIPSEPCHDLEPGTLVPLIPDPAPEFIPERGDRREFINIEVLTRQKL
RVPMAYMNLTSWRPYGARGPSQQPLLHRISHTNYSTVEDWEQHGLVNREHELVVSPHPTN
PVVYELVLINLDDGPHPFHLHGHKFWVLHTGEMEIPAYRYKPEVQREFDLQRAMKRDTVV
VPMLGHAIIRWVADNPGVWAFHCHMLVHLASGMAMAIVEQPTVLQTQPLVPQSCQ

Enzyme Prediction     

No EC number prediction in MGL_3079-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	64	634	4.7e-96	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	2.38e-77	48	639	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	2.10e-70	48	639	24	546	L-ascorbate oxidase
259953	CuRO_2_MCO_like_1	1.94e-68	214	383	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.
259977	CuRO_3_MCO_like_4	1.35e-56	470	639	5	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	3.25e-56	46	639	23	546	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYO41925.1|AA1	0.0	2	655	33	681
AXA49146.1|AA1	0.0	2	655	33	681
AYO41924.1|AA1	6.40e-310	3	654	34	695
AXA49143.1|AA1	6.40e-310	3	654	34	695
CBQ71635.1|AA1	5.08e-126	38	650	52	633

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	2.93e-56	48	639	4	523	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]
1ZPU_A	2.24e-51	50	641	5	481	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]
3V9E_A	4.77e-47	48	639	68	542	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
3SQR_A	1.22e-46	48	639	68	542	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]
1HFU_A	8.19e-46	60	639	17	468	Chain A, LACCASE 1 [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VY90|LAC1_CRYNH	5.63e-64	34	641	48	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|Q55P57|LAC1_CRYNB	2.73e-61	34	642	48	563	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|P14133|ASO_CUCSA	1.32e-60	45	639	36	559	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|J9VQZ4|LAC2_CRYNH	2.09e-60	24	641	28	562	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|Q8LPL3|ASO_ARATH	9.50e-59	52	639	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
1.000057	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGL_3079-t26_1-p1.