CAZyme Information: MGL_3078-t26_1-p1

Basic Information

• Species: Malassezia globosa
• Lineage: Basidiomycota; Malasseziomycetes; ; Malasseziaceae; Malassezia; Malassezia globosa
• CAZyme ID: MGL_3078-t26_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
696		78861.77	6.5457

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=AAYY01000011:13172-15262(-)

Full Sequence      

MGSQSRARTVGYGLVFFLGCALTSAVLWLLYADVDLHGSVHSAWDASTGAFRLGRNTQLV
PATEVTTGPLAMDPSYNASAPPQERFFDWTVERADMAPDGVKRLMYTINGQFPGPMMEVT
EGDTLIVKVRNHIFDNYKVPPPPMSSKLLDVHPEGTDRKISIHWHGLSMRGMQVMDGTSA
VTSCALTPGDEHTYRFVVQPEDVGTHWYHSHVGTSRADGLWGMLIVHAREDERKVLKERA
PAHETHWDEEVAIAVGDHFHDMGPESLARYVSRWLQKAEPVPENALINGKHIFSCHHSRL
SGVPCPAGDVDQVGEYTSFHFRPDRNYRLRLVNVGSLADITFSVDGHTMTVIEADGTLVE
PMKVHRIPISPGQRYSVILHREPDAKMDRMWMRAEMSHECFQYTNPVMELESKAVVAYDG
KTASWKDSQNHMFPLRLRSYRRKVSEFIFQHKRTLKLPTSKAWSPNVTDVGIPTEPCHDL
EPDTLVPLIPDPAPELHLDQGDKREFVYVTVPILEKYSIVPMGFMNGSTWRPYGHRGRDR
QPILHRISHANSTEVEDWYNYDVLEPLHELVASPHPSKPVVFELVINNQDDSPHPFHLHG
HKFWVMETGEMDPQFGGFDYYEDVGQVYPLDRRMKRDTVVVPMMGHAVIRWVADNPGVWA
FHCHMMVHLASGMAMAIVEQPALLQQNPPVPRVCKL

Enzyme Prediction     

No EC number prediction in MGL_3078-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	101	674	7.2e-99	0.9804469273743017

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259953	CuRO_2_MCO_like_1	6.34e-80	251	419	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.
274555	ascorbase	9.72e-76	85	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.
177843	PLN02191	4.59e-71	76	679	17	546	L-ascorbate oxidase
259977	CuRO_3_MCO_like_4	1.36e-66	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	2.88e-57	85	679	25	546	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AXA49143.1|AA1	0.0	1	696	1	697
AYO41924.1|AA1	0.0	1	696	1	697
AXA49146.1|AA1	3.53e-316	14	695	14	681
AYO41925.1|AA1	1.16e-314	14	695	14	681
CBQ71635.1|AA1	9.07e-136	75	688	52	631

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	4.28e-57	83	679	2	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	4.60e-49	87	685	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]
1HFU_A	2.72e-46	90	690	10	481	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	2.77e-46	90	690	10	481	Chain A, Laccase [Coprinopsis cinerea]
5LM8_A	1.82e-44	83	680	24	505	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VQZ4|LAC2_CRYNH	1.29e-63	47	686	22	567	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	1.68e-63	11	684	3	565	Laccase-1 OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) OX=283643 GN=LAC1 PE=1 SV=1
sp|J9VY90|LAC1_CRYNH	1.13e-61	15	684	7	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|P14133|ASO_CUCSA	1.47e-61	82	694	36	574	L-ascorbate oxidase OS=Cucumis sativus OX=3659 PE=1 SV=1
sp|Q40588|ASO_TOBAC	4.00e-58	85	696	31	567	L-ascorbate oxidase OS=Nicotiana tabacum OX=4097 GN=AAO PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999857	0.000173

TMHMM  Annotations     

Start	End
9	31