Annotations: 3M1M

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Prim-pol domain-like	8040772	3001829	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	PF13010	e3m1mA2	A: alpha bundles	X: Primase helical domain (From Topology)	H: Primase helical domain (From Topology)	T: Primase helical domain	F: PF13010	ECOD (1.6)
A	PF09250	e3m1mA1	A: a+b complex topology	X: Prim-pol domain (From Topology)	H: Prim-pol domain (From Topology)	T: Prim-pol domain	F: PF09250	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.720.160	Alpha Beta	2-Layer Sandwich	Signal recognition particle alu RNA binding heterodimer, srp9/1	Bifunctional DNA primase/polymerase, N-terminal	CATH (4.3.0)
A	3.30.2250.10	Alpha Beta	2-Layer Sandwich	Prim-pol fold	Bifunctional DNA primase/polymerase domain	CATH (4.3.0)
A	1.10.1240.50	Mainly Alpha	Orthogonal Bundle	Methyltransferase, Methionine Synthase (B12-binding Domains)	Chain A, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF13010	Primase helical domain (pRN1_helical)	Primase helical domain	This alpha helical domain is found in a set of bacterial plasmid replication proteins [1]. The domain is found to the C-terminus of the primase/polymerase domain. Mutants of this domain are defective in template binding, dinucleotide formation and co ...	This alpha helical domain is found in a set of bacterial plasmid replication proteins [1]. The domain is found to the C-terminus of the primase/polymerase domain. Mutants of this domain are defective in template binding, dinucleotide formation and conformation change prior to DNA extension [1].	Domain
A	PF09250	Bifunctional DNA primase/polymerase, N-terminal (Prim-Pol)	Bifunctional DNA primase/polymerase, N-terminal	Members of this family adopt a structure consisting of a core of antiparallel beta sheets. They are found in various bacterial hypothetical proteins, and have been shown to harbour both primase and polymerase activities [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ORF904	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 hydrolase activity catalytic activity cation binding metal ion binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR014015	Helicase, superfamily 3, DNA virus	Domain
A	IPR014818	Bacteriophage/plasmid primase, P4, C-terminal	Domain
A	IPR006500	Helicase, putative, phage/plasmid, C-terminal domain	Domain
A	IPR045455	NrS-1 polymerase-like, helicase domain	Domain
A	IPR024966	Primase helical domain	Domain
A	IPR015330	DNA primase/polymerase, bifunctional, N-terminal	Domain
A	IPR036390	Winged helix DNA-binding domain superfamily	Homologous Superfamily
A	IPR004968	DNA primase/nucleoside triphosphatase, C-terminal	Domain
A	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.