CAZyme Information: EHY54661.1

Basic Information

• Species: Exophiala dermatitidis
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala dermatitidis
• CAZyme ID: EHY54661.1
• CAZy Family: GH16
• CAZyme Description: laccase TilA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
646	JH226131|CGC1	70307.03	4.6660

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EdermatitidisNIHUT8656	9356	858893	71	9285

• Gene Location: location=JH226131:3773492-3775565(-)

Full Sequence      

MAFSQFITILSFLSLALFSAAAPSSSSSLQKRGDPVKFEVTLTWEDYSPNGGTPRKMIMT
NGTFPGPPLKLKVGDEVEFLVHNDLPDPTAVHFHGIVQQGTPWSDGVPGLTQKPIAPGEC
YLYKWTADAAGVYFYHSHYRSQMMDGMYGAIIISPEKDSDKPFSLISNDTEAIEAMSEAD
ENLQTVFISDYNKYTSQELHEQERSANIDFACADSILLNGQGSQYCLSRDELTAYTNPKV
KALVATVSPSEITDKGCLPPNLAATQGNFTFDIDSIPRDAYFECTPSSGPMATFDVDPAK
GWAALTFINPGGFEMLKFTIDSHKMWVYAVDGGYVVPQLVDQITVNNGDRYSVLIKLDQT
PAQYSIRVSNSGLNQVISGFGILNYKGSTGPAAGEDNPNALAGMNFAGVNLTTLVPFNDN
KAAPYPERAPAPTPDVTYKFNIKKLGQPYGAYDWTLSGIDTFNVTLEDNEQPLLFAKDPN
DIEATDLVLKTNLGQWVDLIVQVQGPLAQPHPMHKHSNKAYVLGKGTGTFNWSTVAEAAA
ELPPNTFNFVNPPLRDGYTTTPAEGNSTWMALRYQVVNPGPFLFHCHMQTHMAGGMAVAF
LDGVDQWPEIPPEYAGPDGDGSGNGITSGATAKLKKKAKLHPKQNE

Enzyme Prediction     

No EC number prediction in EHY54661.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	54	597	1.3e-79	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	1.25e-81	435	603	1	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.
274555	ascorbase	1.54e-64	37	616	5	537	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.
259919	CuRO_1_Abr2_like	9.55e-63	41	153	2	116	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.
259944	CuRO_2_Abr2_like	2.39e-62	184	386	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.
177843	PLN02191	2.42e-58	57	616	43	560	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIW00656.1|AA1	8.81e-228	24	614	26	612
QRC97610.1|AA1	5.71e-219	19	615	26	615
UJO20936.1|AA1	1.08e-191	36	614	24	604
UQC89926.1|AA1	7.12e-190	36	614	39	615
QBZ54343.1|AA1	5.31e-186	36	614	28	604

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AOZ_A	6.60e-50	61	611	28	532	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]
1HFU_A	1.41e-42	40	602	9	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.43e-42	40	602	9	468	Chain A, Laccase [Coprinopsis cinerea]
5Z1X_A	1.51e-41	39	615	7	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]
5LM8_A	5.47e-40	52	602	39	504	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|Q0UHZ8|ELCG_PHANO	1.01e-219	19	615	26	615	Multicopper oxidase elcG OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcG PE=1 SV=1
sp|A0A2G5I8N8|CTB12_CERBT	8.30e-196	36	614	48	624	Multicopper oxidase CTB12 OS=Cercospora beticola OX=122368 GN=CTB12 PE=3 SV=1
sp|E9RBR0|ABR2_ASPFU	1.47e-150	36	617	20	586	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
sp|I1RF62|GIP1_GIBZE	2.13e-150	36	618	25	603	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|A0A1S7IUL2|MCE_TALPI	2.75e-146	39	615	27	593	Multicopper oxidase MCE OS=Talaromyces pinophilus OX=128442 GN=MCE PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000210	0.999764	CS pos: 21-22. Pr: 0.9806

TMHMM  Annotations     

There is no transmembrane helices in EHY54661.1.