1IAW | pdb_00001iaw

CRYSTAL STRUCTURE OF NAEI COMPLEXED WITH 17MER DNA

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
E [auth A]	d1iawa_	Alpha and beta proteins (a/b)	Restriction endonuclease-like	Restriction endonuclease-like	Restriction endonuclease NaeI	Restriction endonuclease NaeI	(Lentzea aerocolonigenes ) [TaxId: 68170 ],	SCOPe (2.08)
F [auth B]	d1iawb_	Alpha and beta proteins (a/b)	Restriction endonuclease-like	Restriction endonuclease-like	Restriction endonuclease NaeI	Restriction endonuclease NaeI	(Lentzea aerocolonigenes ) [TaxId: 68170 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
E [auth A]	SCOP2 Family	Restriction endonuclease NaeI	8021442	4000485	SCOP2 (2022-06-29)
E [auth A]	SCOP2 Superfamily	Restriction endonuclease-like	8033822	3000104	SCOP2 (2022-06-29)
F [auth B]	SCOP2B Superfamily	Restriction endonuclease-like	8033822	3000104	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)
E [auth A]	NaeI_N	e1iawA2	A: a/b three-layered sandwiches	X: Restriction endonuclease-like	H: Restriction endonuclease-like (From Topology)	T: Restriction endonuclease-like	F: NaeI_N	ECOD (1.6)
F [auth B]	NaeI_N	e1iawB2	A: a/b three-layered sandwiches	X: Restriction endonuclease-like	H: Restriction endonuclease-like (From Topology)	T: Restriction endonuclease-like	F: NaeI_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
E [auth A]	3.40.600.10	Alpha Beta	3-Layer(aba) Sandwich	ECO RV Endonuclease	Chain A	CATH (4.3.0)
E [auth A]	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
F [auth B]	3.40.600.10	Alpha Beta	3-Layer(aba) Sandwich	ECO RV Endonuclease	Chain A	CATH (4.3.0)
F [auth B]	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
E [auth A], F [auth B]	PF09126	Restriction endonuclease NaeI (NaeI)	Restriction endonuclease NaeI	Members of this family adopt a secondary structure consisting of nine alpha-helices, six 3-10 helices and 13 beta-strands. They bind two GCC-CGG recognition sequences to cleave DNA into blunt-ended products [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth C], B [auth D], C [auth E], D [auth F]	5'-D(TPGPCPCPAPCPGPCPCPGPGPCPGPTPGPGP*C)-3'	-	-	-
E [auth A], F [auth B]	TYPE II RESTRICTION ENZYME NAEI	DNA binding binding nucleic acid binding endonuclease activity catalytic activity, acting on a nucleic acid hydrolase activity DNA nuclease activity type II site-specific deoxyribonuclease activity restriction endodeoxyribonuclease activity DNA endonuclease activity catalytic activity, acting on DNA nuclease activity hydrolase activity, acting on ester bonds DNA endonuclease activity, producing 5'-phosphomonoesters DNA binding binding nucleic acid binding endonuclease activity catalytic activity, acting on a nucleic acid hydrolase activity DNA nuclease activity type II site-specific deoxyribonuclease activity restriction endodeoxyribonuclease activity DNA endonuclease activity catalytic activity, acting on DNA nuclease activity hydrolase activity, acting on ester bonds DNA endonuclease activity, producing 5'-phosphomonoesters catalytic activity	biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response DNA restriction-modification system defense response to symbiont response to external stimulus primary metabolic process clearance of foreign intracellular DNA clearance of foreign intracellular nucleic acids DNA metabolic process response to biotic stimulus nucleic acid metabolic process nucleobase-containing compound metabolic process DNA modification biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response DNA restriction-modification system defense response to symbiont response to external stimulus primary metabolic process clearance of foreign intracellular DNA clearance of foreign intracellular nucleic acids DNA metabolic process response to biotic stimulus nucleic acid metabolic process nucleobase-containing compound metabolic process DNA modification defense response to other organism response to stress macromolecule modification metabolic process cellular process response to external biotic stimulus macromolecule metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
E [auth A], F [auth B]	IPR011335	Restriction endonuclease type II-like	Homologous Superfamily
E [auth A], F [auth B]	IPR037057	DNA mismatch repair MutH/Type II restriction endonuclease superfamily	Homologous Superfamily
E [auth A], F [auth B]	IPR015210	Type II restriction enzyme NaeI	Domain
E [auth A], F [auth B]	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily

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 R01GM157729.