1Z8S

DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	F_UNCLASSIFIED	e1z8sA2	A: alpha arrays	X: DnaB helicase N-terminal domain-related (From Topology)	H: DnaB helicase N-terminal domain-related (From Topology)	T: DnaB helicase N-terminal domain-related	F: F_UNCLASSIFIED	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.860.10	Mainly Alpha	Orthogonal Bundle	DNAb Helicase	Chain A	CATH (4.3.0)
A	6.10.140.360	Special	Helix non-globular	Helix Hairpins		CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	DNA primase	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 DNA binding nucleic acid binding DNA-directed 5'-3' RNA polymerase activity DNA primase activity 5'-3' RNA polymerase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid RNA polymerase activity transferase activity nucleotidyltransferase activity catalytic activity transferase activity, transferring phosphorus-containing groups cation binding transition metal ion binding zinc ion binding metal ion binding ATP-dependent activity, acting on DNA DNA helicase activity catalytic activity, acting on DNA helicase activity ATP-dependent activity	-	primosome complex protein-containing complex intracellular anatomical structure protein-DNA complex chromosome cellular anatomical entity intracellular organelle organelle intracellular non-membrane-bounded organelle replication fork replisome non-membrane-bounded organelle transferase complex, transferring phosphorus-containing groups catalytic complex primosome complex protein-containing complex intracellular anatomical structure protein-DNA complex chromosome cellular anatomical entity intracellular organelle organelle intracellular non-membrane-bounded organelle replication fork replisome non-membrane-bounded organelle transferase complex, transferring phosphorus-containing groups catalytic complex RNA polymerase complex DNA-directed RNA polymerase complex transferase complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR037068	DNA primase, catalytic core, N-terminal domain superfamily	Homologous Superfamily
A	IPR016136	DNA helicase DnaB, N-terminal/DNA primase DnaG, C-terminal	Homologous Superfamily
A	IPR034151	Bacterial DnaG primase, TOPRIM domain	Domain
A	IPR030846	DNA primase DnaG, bacteria	Family
A	IPR006295	DNA primase, DnaG	Domain
A	IPR006171	TOPRIM domain	Domain
A	IPR002694	Zinc finger, CHC2-type	Domain
A	IPR036977	DNA Primase, CHC2-type zinc finger	Homologous Superfamily
A	IPR013264	DNA primase DNAG, catalytic core, N-terminal	Domain
A	IPR036185	DNA helicase, DnaB-like, N-terminal domain superfamily	Homologous Superfamily
A	IPR019475	DNA primase, DnaB-helicase binding domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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.