Annotations: 4O1R

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4o1ra1	All beta proteins	Hedgehog/intein (Hint) domain	Hedgehog/intein (Hint) domain	Intein (protein splicing domain)	automated matches	(Nostoc punctiforme PCC 73102 ) [TaxId: 63737 ], (Nostoc punctiforme PCC 73102 ) [TaxId: 63737 ],	SCOPe (2.08)
A	d4o1ra2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Nostoc punctiforme PCC 73102 ) [TaxId: 63737 ], (Nostoc punctiforme PCC 73102 ) [TaxId: 63737 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Intein_splicing	e4o1rA1	A: beta complex topology	X: Hedgehog/intein (From Homology)	H: Hedgehog/intein	T: Hint	F: Intein_splicing	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.170.16.10	Mainly Beta	Beta Complex	Endonuclease - Pi-scei	Chain A, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF14890	Intein splicing domain (Intein_splicing)	Intein splicing domain	-	Family
A	PF03796	DnaB-like helicase C terminal domain (DnaB_C)	DnaB-like helicase C terminal domain	The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the q ...	The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerisation of the N-terminal domain has been observed and may occur during the enzymatic cycle. This C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Replicative DNA helicase	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 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 endonuclease activity nuclease activity hydrolase activity, acting on ester bonds ATP-dependent activity, acting on DNA DNA helicase activity catalytic activity, acting on DNA catalytic activity, acting on a nucleic acid helicase activity	intein-mediated protein splicing organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation organic substance metabolic process biosynthetic process proteolysis organic substance biosynthetic process protein processing metabolic process intein-mediated protein splicing organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation organic substance metabolic process biosynthetic process proteolysis organic substance biosynthetic process protein processing metabolic process cellular process protein metabolic process macromolecule metabolic process protein splicing DNA-templated DNA replication DNA replication, synthesis of primer RNA metabolic process DNA metabolic process nucleobase-containing compound biosynthetic process nucleic acid metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process organic cyclic compound metabolic process nucleic acid biosynthetic process DNA replication organic cyclic compound biosynthetic process	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

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036844	Hint domain superfamily	Homologous Superfamily
A	IPR016136	DNA helicase DnaB, N-terminal/DNA primase DnaG, C-terminal	Homologous Superfamily
A	IPR006142	Intein	Domain
A	IPR007693	DNA helicase, DnaB-like, N-terminal	Domain
A	IPR007694	DNA helicase, DnaB-like, C-terminal	Domain
A	IPR004042	Intein DOD homing endonuclease	Domain
A	IPR027434	Homing endonuclease	Homologous Superfamily
A	IPR007692	DNA helicase, DnaB type	Family
A	IPR006141	Intein N-terminal splicing region	PTM
A	IPR004860	Homing endonuclease, LAGLIDADG	Domain
A	IPR003587	Hint domain N-terminal	Domain
A	IPR036185	DNA helicase, DnaB-like, N-terminal domain superfamily	Homologous Superfamily
A	IPR030934	Intein C-terminal splicing region	Domain
A	IPR003586	Hint domain 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.