dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Ophiostoma piceae

Lineage

Ascomycota; Sordariomycetes; ; Ophiostomataceae; Ophiostoma; Ophiostoma piceae

CAZyme ID

EPE06533.1

CAZy Family

GH31

CAZyme Description

Multicopper oxidase [Source:UniProtKB/TrEMBL;Acc:S3CJC5]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
673		72891.28	4.7156

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_OpiceaeUAMH11346	8884	1262450	0	8884

Gene Location

Enzyme Prediction help

EC	1.10.3.2:1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA1	99	275	1.3e-47	0.44692737430167595
AA1	361	652	4.5e-29	0.49162011173184356

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259965	CuRO_3_Abr2_like	1.45e-73	498	658	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.
259919	CuRO_1_Abr2_like	3.60e-49	84	199	1	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.
215324	PLN02604	2.41e-48	78	666	23	555	oxidoreductase
259944	CuRO_2_Abr2_like	3.25e-45	229	439	1	135	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.
274555	ascorbase	1.01e-44	79	666	1	532	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
3.84e-221	62	672	21	632
3.30e-211	74	672	24	638
9.07e-197	82	669	34	600
1.34e-196	78	671	27	601
9.92e-194	78	671	27	601

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.25e-42	93	653	81	538	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
1.07e-41	93	653	81	538	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]
3.43e-41	105	666	27	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]
3.13e-39	83	657	7	472	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]
1.55e-38	92	671	64	543	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.15e-132	82	665	22	579	Laccase abr2 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr2 PE=1 SV=1
3.20e-130	84	670	28	612	Laccase 1 OS=Metarhizium majus (strain ARSEF 297) OX=1276143 GN=Mlac1 PE=3 SV=1
3.44e-129	84	670	27	611	Laccase 1 OS=Metarhizium guizhouense (strain ARSEF 977) OX=1276136 GN=Mlac1 PE=3 SV=1
6.63e-129	84	670	27	611	Laccase 1 OS=Metarhizium anisopliae (strain ARSEF 549) OX=1276135 GN=Mlac1 PE=2 SV=1
2.70e-128	84	670	27	611	Laccase 1 OS=Metarhizium brunneum (strain ARSEF 3297) OX=1276141 GN=Mlac1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.940529	0.059469

TMHMM Annotations help

There is no transmembrane helices in EPE06533.1.

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