Annotations: 3J09

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	HAD-like	8037720	3001890	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	HAD-like	8037720	3001890	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Metal cation-transporting ATPase ATP-binding domain N	8037721	3000981	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	HAD-like	8037720	3001890	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	HAD-like	8037720	3001890	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Metal cation-transporting ATPase ATP-binding domain N	8037721	3000981	SCOP2B (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	E1-E2_ATPase_N	e3j09A3	A: beta sandwiches	X: jelly-roll	H: Calcium ATPase, transduction domain A (From Topology)	T: Calcium ATPase, transduction domain A	F: E1-E2_ATPase_N	ECOD (1.6)
A	E1-E2_ATPase_C	e3j09A4	A: alpha bundles	X: Calcium ATPase transmembrane domain-related (From Homology)	H: Calcium ATPase transmembrane domain-related	T: Copper efflux ATPase transmembrane domain	F: E1-E2_ATPase_C	ECOD (1.6)
A	HMA	e3j09A2	A: a+b two layers	X: Alpha-beta plaits	H: HMA-related	T: HMA, heavy metal-associated domain	F: HMA	ECOD (1.6)
A	P-type_ATPase_Cu-like	e3j09A5	A: a+b complex topology	X: Metal cation-transporting ATPase, ATP-binding domain (From Topology)	H: Metal cation-transporting ATPase, ATP-binding domain (From Topology)	T: Metal cation-transporting ATPase, ATP-binding domain	F: P-type_ATPase_Cu-like	ECOD (1.6)
A	Hydrolase_3_1	e3j09A1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: Hydrolase_3_1	ECOD (1.6)
B	E1-E2_ATPase_N	e3j09B6	A: beta sandwiches	X: jelly-roll	H: Calcium ATPase, transduction domain A (From Topology)	T: Calcium ATPase, transduction domain A	F: E1-E2_ATPase_N	ECOD (1.6)
B	E1-E2_ATPase_C	e3j09B4	A: alpha bundles	X: Calcium ATPase transmembrane domain-related (From Homology)	H: Calcium ATPase transmembrane domain-related	T: Copper efflux ATPase transmembrane domain	F: E1-E2_ATPase_C	ECOD (1.6)
B	HMA	e3j09B7	A: a+b two layers	X: Alpha-beta plaits	H: HMA-related	T: HMA, heavy metal-associated domain	F: HMA	ECOD (1.6)
B	P-type_ATPase_Cu-like	e3j09B5	A: a+b complex topology	X: Metal cation-transporting ATPase, ATP-binding domain (From Topology)	H: Metal cation-transporting ATPase, ATP-binding domain (From Topology)	T: Metal cation-transporting ATPase, ATP-binding domain	F: P-type_ATPase_Cu-like	ECOD (1.6)
B	Hydrolase_3_1	e3j09B8	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: Hydrolase_3_1	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00403	Heavy-metal-associated domain (HMA)	Heavy-metal-associated domain	-	Domain
A, B	PF00702	haloacid dehalogenase-like hydrolase (Hydrolase)	haloacid dehalogenase-like hydrolase	This family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted fo ...	This family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain [1]. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria [2].	Domain
A, B	PF00122	E1-E2 ATPase (E1-E2_ATPase)	E1-E2 ATPase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	copper-exporting P-type ATPase A	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity ATP-dependent activity cation binding transition metal ion binding copper ion binding metal ion binding identical protein binding protein binding monoatomic cation transmembrane transporter activity P-type transmembrane transporter activity primary active transmembrane transporter activity ATPase-coupled transmembrane transporter activity copper ion transmembrane transporter activity ATPase-coupled monoatomic cation transmembrane transporter activity P-type ion transporter activity P-type monovalent copper transporter activity active monoatomic ion transmembrane transporter activity active transmembrane transporter activity inorganic molecular entity transmembrane transporter activity inorganic cation transmembrane transporter activity monoatomic ion transmembrane transporter activity transporter activity transition metal ion transmembrane transporter activity metal ion transmembrane transporter activity transmembrane transporter activity	-	cell periphery plasma membrane membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR017969	Heavy-metal-associated, conserved site	Conserved Site
A, B	IPR023214	HAD superfamily	Homologous Superfamily
A, B	IPR006121	Heavy metal-associated domain, HMA	Domain
A, B	IPR008250	P-type ATPase, A domain superfamily	Homologous Superfamily
A, B	IPR001757	P-type ATPase	Family
A, B	IPR044492	P-type ATPase, haloacid dehalogenase domain	Domain
A, B	IPR027256	P-type ATPase, subfamily IB	Family
A, B	IPR018303	P-type ATPase, phosphorylation site	PTM
A, B	IPR036412	HAD-like superfamily	Homologous Superfamily
A, B	IPR023298	P-type ATPase, transmembrane domain superfamily	Homologous Superfamily
A, B	IPR006122	Heavy metal-associated domain, copper ion-binding	Domain
A, B	IPR036163	Heavy metal-associated domain superfamily	Homologous Superfamily
A, B	IPR023299	P-type ATPase, cytoplasmic domain N	Homologous Superfamily

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B	OPM	Transmembrane	Alpha-helical polytopic	P-type ATPase (P-ATPase)	Copper-transporting P-type ATPase

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A, B	MemProtMD	Annotated as membrane protein by MemProtMD

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.