Annotations: 1RR9

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1rr9a_	Alpha and beta proteins (a+b)	Ribosomal protein S5 domain 2-like	Ribosomal protein S5 domain 2-like	ATP-dependent protease Lon (La), catalytic domain	ATP-dependent protease Lon (La), catalytic domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1rr9b_	Alpha and beta proteins (a+b)	Ribosomal protein S5 domain 2-like	Ribosomal protein S5 domain 2-like	ATP-dependent protease Lon (La), catalytic domain	ATP-dependent protease Lon (La), catalytic domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1rr9c_	Alpha and beta proteins (a+b)	Ribosomal protein S5 domain 2-like	Ribosomal protein S5 domain 2-like	ATP-dependent protease Lon (La), catalytic domain	ATP-dependent protease Lon (La), catalytic domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1rr9d_	Alpha and beta proteins (a+b)	Ribosomal protein S5 domain 2-like	Ribosomal protein S5 domain 2-like	ATP-dependent protease Lon (La), catalytic domain	ATP-dependent protease Lon (La), catalytic domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
F	d1rr9f_	Alpha and beta proteins (a+b)	Ribosomal protein S5 domain 2-like	Ribosomal protein S5 domain 2-like	ATP-dependent protease Lon (La), catalytic domain	ATP-dependent protease Lon (La), catalytic domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E	d1rr9e_	Alpha and beta proteins (a+b)	Ribosomal protein S5 domain 2-like	Ribosomal protein S5 domain 2-like	ATP-dependent protease Lon (La), catalytic domain	ATP-dependent protease Lon (La), catalytic domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8040879	3000100	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8040879	3000100	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8040879	3000100	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8040879	3000100	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8040879	3000100	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8040879	3000100	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	Lon_C_N	e1rr9A1	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Lon_C_N	ECOD (1.6)
A	Lon_C_C	e1rr9A2	A: a/b three-layered sandwiches	X: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	H: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	T: C-terminal subdomain in Lon-related proteases catalytic domains	F: Lon_C_C	ECOD (1.6)
B	Lon_C_N	e1rr9B1	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Lon_C_N	ECOD (1.6)
B	Lon_C_C	e1rr9B2	A: a/b three-layered sandwiches	X: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	H: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	T: C-terminal subdomain in Lon-related proteases catalytic domains	F: Lon_C_C	ECOD (1.6)
C	Lon_C_N	e1rr9C1	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Lon_C_N	ECOD (1.6)
C	Lon_C_C	e1rr9C2	A: a/b three-layered sandwiches	X: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	H: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	T: C-terminal subdomain in Lon-related proteases catalytic domains	F: Lon_C_C	ECOD (1.6)
D	Lon_C_N	e1rr9D1	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Lon_C_N	ECOD (1.6)
D	Lon_C_C	e1rr9D2	A: a/b three-layered sandwiches	X: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	H: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	T: C-terminal subdomain in Lon-related proteases catalytic domains	F: Lon_C_C	ECOD (1.6)
F	Lon_C_N	e1rr9F1	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Lon_C_N	ECOD (1.6)
F	Lon_C_C	e1rr9F2	A: a/b three-layered sandwiches	X: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	H: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	T: C-terminal subdomain in Lon-related proteases catalytic domains	F: Lon_C_C	ECOD (1.6)
E	Lon_C_N	e1rr9E1	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Lon_C_N	ECOD (1.6)
E	Lon_C_C	e1rr9E2	A: a/b three-layered sandwiches	X: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	H: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	T: C-terminal subdomain in Lon-related proteases catalytic domains	F: Lon_C_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.230.10	Alpha Beta	2-Layer Sandwich	Ribosomal Protein S5	domain 2	CATH (4.3.0)
B	3.30.230.10	Alpha Beta	2-Layer Sandwich	Ribosomal Protein S5	domain 2	CATH (4.3.0)
C	3.30.230.10	Alpha Beta	2-Layer Sandwich	Ribosomal Protein S5	domain 2	CATH (4.3.0)
D	3.30.230.10	Alpha Beta	2-Layer Sandwich	Ribosomal Protein S5	domain 2	CATH (4.3.0)
F	3.30.230.10	Alpha Beta	2-Layer Sandwich	Ribosomal Protein S5	domain 2	CATH (4.3.0)
E	3.30.230.10	Alpha Beta	2-Layer Sandwich	Ribosomal Protein S5	domain 2	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	ATP-dependent protease La	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity endopeptidase activity sequence-specific DNA binding DNA binding binding organic cyclic compound binding nucleic acid binding adenyl ribonucleotide binding peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity endopeptidase activity sequence-specific DNA binding DNA binding binding organic cyclic compound binding nucleic acid binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity, acting on acid anhydrides ATP-dependent activity ATP-dependent peptidase activity	cellular response to stimulus cellular response to heat response to stimulus cellular response to stress response to stress response to heat response to abiotic stimulus cellular process response to temperature stimulus response to X-ray response to ionizing radiation response to radiation proteolysis metabolic process cellular response to stimulus cellular response to heat response to stimulus cellular response to stress response to stress response to heat response to abiotic stimulus cellular process response to temperature stimulus response to X-ray response to ionizing radiation response to radiation proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process catabolic process proteolysis involved in protein catabolic process protein catabolic process protein quality control for misfolded or incompletely synthesized proteins macromolecule catabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR015947	PUA-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR046336	Lon protease, N-terminal domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR003593	AAA+ ATPase domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR027065	Lon protease	Family
A, B, C, D, E A, B, C, D, E, F	IPR008268	Peptidase S16, active site	Active Site
A, B, C, D, E A, B, C, D, E, F	IPR003959	ATPase, AAA-type, core	Domain
A, B, C, D, E A, B, C, D, E, F	IPR020568	Ribosomal protein uS5 domain 2-type superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR014721	Small ribosomal subunit protein uS5 domain 2-type fold, subgroup	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR027543	Lon protease, bacterial	Family
A, B, C, D, E A, B, C, D, E, F	IPR003111	Lon protease, N-terminal domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR004815	Lon protease, bacterial/eukaryotic-type	Family
A, B, C, D, E A, B, C, D, E, F	IPR008269	Peptidase S16, Lon proteolytic 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 R01GM157729.