Annotations: 1A65

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1a65a3	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Laccase, C-terminal domain	(Coprinopsis cinerea ) [TaxId: 5346 ],	SCOPe (2.08)
A	d1a65a2	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Laccase, middle domain	(Coprinopsis cinerea ) [TaxId: 5346 ],	SCOPe (2.08)
A	d1a65a1	All beta proteins	Cupredoxin-like	Cupredoxins	Multidomain cupredoxins	Laccase, N-terminal domain	(Coprinopsis cinerea ) [TaxId: 5346 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Multidomain cupredoxins	8028309	4002203	SCOP2 (2022-06-29)
A	SCOP2 Family	Multidomain cupredoxins	8028311	4002203	SCOP2 (2022-06-29)
A	SCOP2 Family	Multidomain cupredoxins	8028312	4002203	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Cupredoxins	8040688	3000886	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Cupredoxins	8040690	3000886	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Cupredoxins	8040691	3000886	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Cu-oxidase_2	e1a65A3	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_2	ECOD (1.6)
A	Cu-oxidase_3	e1a65A1	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase_3	ECOD (1.6)
A	Cu-oxidase	e1a65A2	A: beta sandwiches	X: Cupredoxin-like	H: Cupredoxin-related (From Topology)	T: Cupredoxin-related	F: Cu-oxidase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.420	Mainly Beta	Sandwich	Immunoglobulin-like	Cupredoxins - blue copper proteins	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00394	Multicopper oxidase (Cu-oxidase)	Multicopper oxidase	Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain.	Domain
A	PF07732	Multicopper oxidase (Cu-oxidase_3)	Multicopper oxidase	This entry contains many divergent copper oxidase-like domains that are not recognised by the Pfam:PF00394 model.	Domain
A	PF07731	Multicopper oxidase (Cu-oxidase_2)	Multicopper oxidase	This entry contains many divergent copper oxidase-like domains that are not recognised by the Pfam:PF00394 model.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	LACCASE	cation binding transition metal ion binding copper ion binding ion binding binding metal ion binding small molecule binding oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor oxidoreductase activity oxidoreductase activity, acting on diphenols and related substances as donors hydroquinone:oxygen oxidoreductase activity catalytic activity	-	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR008972	Cupredoxin	Homologous Superfamily
A	IPR002355	Multicopper oxidase, copper-binding site	Binding Site
A	IPR001117	Multicopper oxidase, second cupredoxin domain	Domain
A	IPR011706	Multicopper oxidase, C-terminal	Domain
A	IPR045087	Multicopper oxidase	Family
A	IPR033138	Multicopper oxidases, conserved site	Conserved Site
A	IPR011707	Multicopper oxidase-like, N-terminal	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.