Annotations: 2FOK

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2foka1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	Restriction endonuclease FokI, N-terminal (recognition) domain	Restriction endonuclease FokI, N-terminal (recognition) domain	(Planomicrobium okeanokoites ) [TaxId: 244 ],	SCOPe (2.08)
A	d2foka4	Alpha and beta proteins (a/b)	Restriction endonuclease-like	Restriction endonuclease-like	Restriction endonuclease FokI, C-terminal (catalytic) domain	Restriction endonuclease FokI, C-terminal (catalytic) domain	(Planomicrobium okeanokoites ) [TaxId: 244 ],	SCOPe (2.08)
B	d2fokb1	All alpha proteins	DNA/RNA-binding 3-helical bundle	'Winged helix' DNA-binding domain	Restriction endonuclease FokI, N-terminal (recognition) domain	Restriction endonuclease FokI, N-terminal (recognition) domain	(Planomicrobium okeanokoites ) [TaxId: 244 ],	SCOPe (2.08)
B	d2fokb4	Alpha and beta proteins (a/b)	Restriction endonuclease-like	Restriction endonuclease-like	Restriction endonuclease FokI, C-terminal (catalytic) domain	Restriction endonuclease FokI, C-terminal (catalytic) domain	(Planomicrobium okeanokoites ) [TaxId: 244 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Winged helix DNA-binding domain	8002918	3000034	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Winged helix DNA-binding domain	8002916	3000034	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Restriction endonuclease-like	8002914	3000104	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Winged helix DNA-binding domain	8002920	3000034	SCOP2B (2022-06-29)
B	SCOP2 Family	FokI recognition domain-like	8091677	4000174	SCOP2 (2022-06-29)
B	SCOP2 Family	FokI catalytic domain-like	8002913	4000280	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Winged helix DNA-binding domain	8002916	3000034	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Winged helix DNA-binding domain	8002918	3000034	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Winged helix DNA-binding domain	8002920	3000034	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Restriction endonuclease-like	8002914	3000104	SCOP2 (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	FokI_C	e2fokA2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: FokI_C	ECOD (1.6)
A	FokI_N	e2fokA1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: FokI_N	ECOD (1.6)
A	Type2_restr_D3	e2fokA3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: Type2_restr_D3	ECOD (1.6)
A	Endonuc-FokI_C	e2fokA4	A: a/b three-layered sandwiches	X: Restriction endonuclease-like	H: Restriction endonuclease-like (From Topology)	T: Restriction endonuclease-like	F: Endonuc-FokI_C	ECOD (1.6)
B	FokI_C	e2fokB2	A: alpha arrays	X: HTH	H: HTH	T: winged	F: FokI_C	ECOD (1.6)
B	FokI_N	e2fokB1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: FokI_N	ECOD (1.6)
B	Type2_restr_D3	e2fokB3	A: alpha arrays	X: HTH	H: HTH	T: winged	F: Type2_restr_D3	ECOD (1.6)
B	Endonuc-FokI_C	e2fokB4	A: a/b three-layered sandwiches	X: Restriction endonuclease-like	H: Restriction endonuclease-like (From Topology)	T: Restriction endonuclease-like	F: Endonuc-FokI_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.241.10	Alpha Beta	Alpha-Beta Complex	FokI Restriction Endonuclease	Chain A, domain 1	CATH (4.3.0)
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)
A	3.40.91.30	Alpha Beta	3-Layer(aba) Sandwich	Restriction Endonuclease		CATH (4.3.0)
B	3.90.241.10	Alpha Beta	Alpha-Beta Complex	FokI Restriction Endonuclease	Chain A, domain 1	CATH (4.3.0)
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)
B	3.40.91.30	Alpha Beta	3-Layer(aba) Sandwich	Restriction Endonuclease		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF16902	FokI, D3 domain (FokI_D3)	FokI, D3 domain	Type IIS restriction endonuclease FokI is a member of an unusual class of bipartite restriction enzymes that recognises the double- stranded DNA sequence 5'-GGATG-3' and cleave DNA phosphodiester groups 9 base pairs away on this strand and 13 base pa ...	Type IIS restriction endonuclease FokI is a member of an unusual class of bipartite restriction enzymes that recognises the double- stranded DNA sequence 5'-GGATG-3' and cleave DNA phosphodiester groups 9 base pairs away on this strand and 13 base pairs away on the complementary strand [1,2]. FokI contains amino- and carboxy- terminal domains corresponding to the DNA-recognition and cleavage functions, respectively. The recognition domain is made of three smaller subdomains (D1, D2 and D3) which are evolutionarily related to the helix-turn-helix-containing DNA-binding domain of the catabolite gene activator protein CAP [1]. This is the D3 domain which is most similar to CAP and related proteins such as histone H5, HNF-3gamma and the biotin operon repressor (BirA). Despite its similarity, D3 barely touches the DNA [1].	Domain
A, B	PF09254	FokI, cleavage domain (FokI_cleav_dom)	FokI, cleavage domain	Members of this family are predominantly found in prokaryotic restriction endonuclease FokI, and adopt a structure consisting of an alpha/beta/alpha core containing a five-stranded beta-sheet. They recognise the double-stranded DNA sequence 5'-GGATG- ...	Members of this family are predominantly found in prokaryotic restriction endonuclease FokI, and adopt a structure consisting of an alpha/beta/alpha core containing a five-stranded beta-sheet. They recognise the double-stranded DNA sequence 5'-GGATG-3' and cleave DNA phosphodiester groups 9 base pairs away on this strand and 13 base pairs away on the complementary strand [1]. This entry represents the C-terminal cleavage domain of FokI.	Domain
A, B	PF02980	FokI, recognition domain, subdomain 2 (FokI_dom_2)	FokI, recognition domain, subdomain 2	Type IIS restriction endonuclease FokI is a member of an unusual class of bipartite restriction enzymes that recognises the double-stranded DNA sequence 5'-GGATG-3' and cleave DNA phosphodiester groups 9 base pairs away on this strand and 13 base pai ...	Type IIS restriction endonuclease FokI is a member of an unusual class of bipartite restriction enzymes that recognises the double-stranded DNA sequence 5'-GGATG-3' and cleave DNA phosphodiester groups 9 base pairs away on this strand and 13 base pairs away on the complementary strand [1]. FokI contains amino- and carboxy-terminal domains corresponding to the DNA- recognition and cleavage functions, respectively. The recognition domain is made of three smaller subdomains (D1, D2 and D3) which are evolutionarily related to the helix-turn-helix-containing DNA-binding domain of the catabolite gene activator protein CAP [3]. This entry represents the subdomain D2 of FokI. D1 and D2 make almost all of the base-specific contacts with the DNA [3].	Domain
A, B	PF02981	FokI, recognition domain, subdomain 1 (FokI_D1)	FokI, recognition domain, subdomain 1	Type IIS restriction endonuclease FokI is a member of an unusual class of bipartite restriction enzymes that recognises the double-stranded DNA sequence 5'-GGATG-3' and cleave DNA phosphodiester groups 9 base pairs away on this strand and 13 base pai ...	Type IIS restriction endonuclease FokI is a member of an unusual class of bipartite restriction enzymes that recognises the double-stranded DNA sequence 5'-GGATG-3' and cleave DNA phosphodiester groups 9 base pairs away on this strand and 13 base pairs away on the complementary strand [1]. FokI contains amino- and carboxy-terminal domains corresponding to the DNA- recognition and cleavage functions, respectively. The recognition domain is made of three smaller subdomains (D1, D2 and D3) which are evolutionarily related to the helix-turn-helix- containing DNA-binding domain of the catabolite gene activator protein CAP [3]. This entry represents the subdomain D1 of FokI. Subdomain D1 of the recognition domain covers the DNA major groove, recognizing base pairs at the 3' end of the recognition sequence (GGATG) [3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	FOKI RESTRICTION ENDONUCLEASE	DNA binding binding organic cyclic compound binding nucleic acid binding endonuclease activity catalytic activity, acting on a nucleic acid endodeoxyribonuclease activity, producing 5'-phosphomonoesters hydrolase activity DNA nuclease activity type II site-specific deoxyribonuclease activity restriction endodeoxyribonuclease activity DNA endonuclease activity nuclease activity hydrolase activity, acting on ester bonds DNA binding binding organic cyclic compound binding nucleic acid binding endonuclease activity catalytic activity, acting on a nucleic acid endodeoxyribonuclease activity, producing 5'-phosphomonoesters hydrolase activity DNA nuclease activity type II site-specific deoxyribonuclease activity restriction endodeoxyribonuclease activity DNA endonuclease activity nuclease activity hydrolase activity, acting on ester bonds catalytic activity, acting on DNA endonuclease activity, active with either ribo- or deoxyribonucleic acids and producing 5'-phosphomonoesters catalytic activity	biological process involved in interspecies interaction between organisms response to stimulus DNA restriction-modification system clearance of foreign intracellular nucleic acids response to biotic stimulus nucleobase-containing compound metabolic process DNA modification organic substance metabolic process response to stress response to external biotic stimulus response to other organism defense response defense response to symbiont response to external stimulus biological process involved in interspecies interaction between organisms response to stimulus DNA restriction-modification system clearance of foreign intracellular nucleic acids response to biotic stimulus nucleobase-containing compound metabolic process DNA modification organic substance metabolic process response to stress response to external biotic stimulus response to other organism defense response defense response to symbiont response to external stimulus primary metabolic process clearance of foreign intracellular DNA DNA metabolic process nucleic acid metabolic process organic cyclic compound metabolic process defense response to other organism macromolecule modification metabolic process macromolecule metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR004234	FokI, recognition domain, subdomain 1	Domain
A, B	IPR015334	FokI, cleavage domain	Domain
A, B	IPR011335	Restriction endonuclease type II-like	Homologous Superfamily
A, B	IPR004233	FokI, recognition domain, subdomain 2	Domain
A, B	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily
A, B	IPR036390	Winged helix DNA-binding domain superfamily	Homologous Superfamily
A, B	IPR031655	FokI, D3 domain	Domain
A, B	IPR044945	FokI, recognition domain, subdomain 1 and 2	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	type II site-specific deoxyribonuclease FokI M-CSA #927	FokI is a member an unusual class of restriction enzymes that recognise a specific DNA sequence and cleave non-specifically a short distance away from that sequence. FokI consists of an N-terminal DNA recognition domain and a C-terminal cleavage domain.	Defined by 3 residues: ASP:A-450ASP:A-467LYS:A-469 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.1.21.4 (PDB Primary Data) Search M-CSA Motif + EC 3.1.21.4

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.