Annotations: 3EZ2

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	ParA N-terminal domain-like-like	8058204	4007683	SCOP2 (2022-06-29)
A	SCOP2 Family	CobQ/CobB/MinD/ParA nucleotide binding domain-like	8017791	4003982	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Putative DNA-binding domain	8017789	3000158	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Simibi-like P-loop NTPases	8017792	3002018	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Simibi-like P-loop NTPases	8017792	3002018	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Putative DNA-binding domain	8017789	3000158	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	PF18607	e3ez2A5	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: PF18607	ECOD (1.6)
A	PF13614	e3ez2A4	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF13614	ECOD (1.6)
B	PF18607	e3ez2B2	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: PF18607	ECOD (1.6)
B	PF13614	e3ez2B3	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF13614	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.1660.30	Mainly Alpha	Orthogonal Bundle	Multidrug-efflux Transporter Regulator	Chain: A	CATH (4.3.0)
A	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
B	1.10.1660.30	Mainly Alpha	Orthogonal Bundle	Multidrug-efflux Transporter Regulator	Chain: A	CATH (4.3.0)
B	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF13614	AAA domain (AAA_31)	AAA domain	This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.	Domain
A, B	PF18607	ParA helix turn helix domain (HTH_54)	ParA helix turn helix domain	The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregati ...	The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregation by interacting with centromere-bound ParB, but when bound to ADP, ParA fulfills a different function: DNA-binding transcription autoregulation. ParA consists of an elongated N-terminal alpha-helix which mediates dimerization, a winged-HTH and a Walker-box containing C-domain. This entry describes the N-terminal alpha helix domain combined with the winged HTH region [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Plasmid partition protein A	identical protein binding protein binding binding	plasmid partitioning cellular process plasmid maintenance	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR025669	AAA domain	Domain
A, B	IPR041250	ParA helix turn helix domain	Domain
A, B	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

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.