Annotations: 2H6J

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d2h6jb1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
C	d2h6jc1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
F	d2h6jf1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
G	d2h6jg1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
A	d2h6ja1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
D	d2h6jd1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
E	d2h6je1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
K	d2h6jk1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
M	d2h6jm1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
N	d2h6jn1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
H	d2h6jh1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
I	d2h6ji1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
J	d2h6jj1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)
L	d2h6jl1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome beta subunit (catalytic)	(Rhodococcus erythropolis ) [TaxId: 1833 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Class II glutamine amidotransferases	8039779	3000131	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Class II glutamine amidotransferases	8039779	3000131	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Class II glutamine amidotransferases	8039779	3000131	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Class II glutamine amidotransferases	8039779	3000131	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Class II glutamine amidotransferases	8039779	3000131	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Class II glutamine amidotransferases	8039779	3000131	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Class II glutamine amidotransferases	8039779	3000131	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	Class II glutamine amidotransferases	8039790	3000131	SCOP2B (2022-06-29)
M	SCOP2B Superfamily	Class II glutamine amidotransferases	8039790	3000131	SCOP2B (2022-06-29)
N	SCOP2B Superfamily	Class II glutamine amidotransferases	8039790	3000131	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Class II glutamine amidotransferases	8039790	3000131	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Class II glutamine amidotransferases	8039790	3000131	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	Class II glutamine amidotransferases	8039790	3000131	SCOP2B (2022-06-29)
L	SCOP2B Superfamily	Class II glutamine amidotransferases	8039790	3000131	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)
B	PF00227	e2h6jB1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
C	PF00227	e2h6jC1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
F	PF00227	e2h6jF1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
G	PF00227	e2h6jG1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
A	PF00227	e2h6jA1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
D	PF00227	e2h6jD1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
E	PF00227	e2h6jE1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
K	PF00227	e2h6jK1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
M	PF00227	e2h6jM1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
N	PF00227	e2h6jN1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
H	PF00227	e2h6jH1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
I	PF00227	e2h6jI1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
J	PF00227	e2h6jJ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
L	PF00227	e2h6jL1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
C	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
F	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
G	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
A	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
D	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
E	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
K	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
M	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
N	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
H	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
I	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
J	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)
L	3.60.20.10	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	Aminohydrolase, N-terminal nucleophile (Ntn) domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain

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, G	Proteasome alpha-type subunit 1	peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity hydrolase activity catalytic activity endopeptidase activity threonine-type endopeptidase activity	organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process organic substance catabolic process proteasomal protein catabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity protein-containing complex proteasome core complex, alpha-subunit complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex
H, I, J, K, L H, I, J, K, L, M, N	Proteasome beta-type subunit 1	peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity hydrolase activity catalytic activity endopeptidase activity threonine-type endopeptidase activity	organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process organic substance catabolic process proteasomal protein catabolic process	protein-containing complex intracellular anatomical structure catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex cellular anatomical entity intracellular protein-containing complex proteasome core complex, beta-subunit complex cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G	IPR022296	Proteasome, alpha subunit, bacterial	Family
A, B, C, D, E A, B, C, D, E, F, G	IPR023332	Proteasome alpha-type subunit	Family
A, B, C, D, E A, B, C, D, E, F, G	IPR001353	Proteasome, subunit alpha/beta	Family
H, I, J, K, L H, I, J, K, L, M, N	IPR023333	Proteasome B-type subunit	Family
H, I, J, K, L H, I, J, K, L, M, N	IPR022483	Proteasome subunit beta, actinobacteria	Family
H, I, J, K, L H, I, J, K, L, M, N	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
H, I, J, K, L H, I, J, K, L, M, N	IPR001353	Proteasome, subunit alpha/beta	Family

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.