CAZyme Information: GBF64015.1

Basic Information

• Species: Trichophyton mentagrophytes
• Lineage: Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Trichophyton; Trichophyton mentagrophytes
• CAZyme ID: GBF64015.1
• CAZy Family: GH43
• CAZyme Description: multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
603	BFBS01016332|CGC2	68285.25	6.1081

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmentagrophytesTIMM2789	7958	N/A	98	7860

• Gene Location: location=BFBS01016332:33925-36092(+)

Full Sequence      

MRGWIIDLCALTAGEAAAKVVHEELTLTWGLGAPNGQPREMIFMNGQFPGPTFVWDEDDD
VEVLVHNKMPFNTTIHWHGLLMQGTPWSDGVPGLTQKPIEVGESFIYRFKAYPSGTHWWH
SHTRTTMFDGLFGAMYIRPKPTAPAPWSLISNDQKDIGSMKKAVANPHVVVVSDWTRFKS
WEYMKAQEDSGYTIFCVDSILINGKGSVYCPGEDFLVNHTMDYMKWAIYPRHVNDKGCLP
FVKSTENKYLRDGHPETIPLHLQQGCVQSEGEQAVFEVDPADEWVSFNFVDAATFKTPVF
AIDEHEMWVYEADGHFIEPQKVDTVKFYAGERYSVMVKLRKNDSRDYTIRVMDTGLTQII
GSYATLRYKRSPNDKNVHEAKESKGILNYGGLNTTHVVTLDRDNLPPYPPNAPAAHADAL
YLLDTHRVKTAWTYTMKGGAMYQEDRSAYAPLLYYPDSADAMDDSLVIRTKNNTWIDLVV
QVGSLPNQPQEFPHIMHKHSGKTWQIGAGEGHWNYSSVEEAMKAEPTKFNLKTPNYRDTF
ITSFDGPSWIVLRYHSNNPGPWLMHCHFEIHLGGGMAIAFMDGVDAWPKVPPEYAPGKGG
FLE

Enzyme Prediction     

No EC number prediction in GBF64015.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	38	577	1.1e-80	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	6.58e-80	420	583	3	164	The third cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase 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 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.
259944	CuRO_2_Abr2_like	1.23e-63	168	369	1	138	The second cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase 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.
259919	CuRO_1_Abr2_like	6.71e-56	24	138	2	117	The first cupredoxin domain of a group of fungal Laccases similar to Abr2 from Aspergillus fumigatus. Abr2 is involved in conidial pigment biosynthesis in Aspergillus fumigatus. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. Laccase has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Like other related multicopper oxidases (MCOs), laccase 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 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
274555	ascorbase	1.05e-52	31	593	12	534	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.
215324	PLN02604	2.63e-48	8	591	12	555	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CEI66207.1|AA1	2.48e-311	17	602	21	603
QKX57114.1|AA1	1.09e-310	1	602	1	603
CZS77880.1|AA1	2.66e-307	17	602	21	608
CEF74605.1|AA1	7.60e-307	17	602	21	608
QKG86291.1|AA1	3.24e-297	13	601	17	567

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	9.12e-46	18	593	1	534	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]
5Z1X_A	4.85e-39	33	595	16	478	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
3KW7_A	5.66e-37	24	592	7	482	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
1HFU_A	5.74e-37	23	582	7	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	5.81e-37	23	582	7	468	Chain A, Laccase [Coprinopsis cinerea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RF62|GIP1_GIBZE	1.35e-307	17	602	21	608	Multicopper oxidase GIP1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=GIP1 PE=1 SV=1
sp|A0A443HK79|VDTB1_BYSSP	1.02e-238	21	603	20	606	Multicopper oxidase VdtB OS=Byssochlamys spectabilis OX=264951 GN=VdtB PE=1 SV=1
sp|A0A1S7IUL2|MCE_TALPI	9.05e-227	14	600	17	598	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1
sp|A0A4Y6F0M8|USTL_USTVR	5.82e-220	1	595	4	606	Laccase ustL OS=Ustilaginoidea virens OX=1159556 GN=ustL PE=1 SV=1
sp|A0A0B4F1I0|MLAC1_METAF	2.08e-202	5	594	7	610	Laccase 1 OS=Metarhizium anisopliae (strain ARSEF 549) OX=1276135 GN=Mlac1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999803	0.000261

TMHMM  Annotations     

There is no transmembrane helices in GBF64015.1.