Annotations: 6Z46

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
C [auth B]	SCOP2 Family	Proteasome subunits	8096311	4002254	SCOP2 (2022-06-29)
C [auth B]	SCOP2 Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2 (2022-06-29)
D [auth C]	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
E [auth D]	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
F [auth E]	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
G [auth F]	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
H [auth G]	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
O	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
P	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
Q	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
S	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
T	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
U	SCOP2B Superfamily	Class II glutamine amidotransferases	8096312	3000131	SCOP2B (2022-06-29)
AA [auth a]	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
B [auth H]	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
BA [auth b]	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
L	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
M	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
N	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
V	SCOP2 Family	Proteasome subunits	8096313	4002254	SCOP2 (2022-06-29)
V	SCOP2 Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2 (2022-06-29)
W	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
X	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
Y	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	3000131	SCOP2B (2022-06-29)
Z	SCOP2B Superfamily	Class II glutamine amidotransferases	8096314	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)
A	PF00227,PF10584	e6z46A1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
C [auth B]	PF00227,PF10584	e6z46B1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
D [auth C]	PF00227,PF10584	e6z46C1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
E [auth D]	PF00227,PF10584	e6z46D1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
F [auth E]	PF00227,PF10584	e6z46E1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
G [auth F]	PF00227,PF10584	e6z46F1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
H [auth G]	PF00227,PF10584	e6z46G1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
O	PF00227,PF10584	e6z46O1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
P	PF00227,PF10584	e6z46P1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
Q	PF00227,PF10584	e6z46Q1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
R	PF00227,PF10584	e6z46R1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
S	PF00227,PF10584	e6z46S1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
T	PF00227,PF10584	e6z46T1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
U	PF00227,PF10584	e6z46U1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227,PF10584	ECOD (1.6)
AA [auth a]	PF00227	e6z46a1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
B [auth H]	PF00227	e6z46H1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
BA [auth b]	PF00227	e6z46b1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
I	PF00227	e6z46I1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
J	PF00227	e6z46J1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
K	PF00227	e6z46K1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
L	PF00227	e6z46L1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
M	PF00227	e6z46M1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
N	PF00227	e6z46N1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
V	PF00227	e6z46V1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
W	PF00227	e6z46W1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
X	PF00227	e6z46X1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
Y	PF00227	e6z46Y1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)
Z	PF00227	e6z46Z1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: PF00227	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], O, P, Q, R, S, T, U	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
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], O, P, Q, R, S, T, U	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
AA [auth a], B [auth H], BA [auth b], I, J, AA [auth a], B [auth H], BA [auth b], I, J, K, L, M, N, V, W, X, Y, Z	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, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], O, P, Q, R, S, T, U	Proteasome subunit alpha	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 ubiquitin-dependent protein catabolic process metabolic process protein 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 ubiquitin-dependent protein catabolic process 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
AA [auth a], B [auth H], BA [auth b], I, J, AA [auth a], B [auth H], BA [auth b], I, J, K, L, M, N, V, W, X, Y, Z	Proteasome subunit beta	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 proteasomal protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process organic substance 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, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], O, P, Q, R, S, T, U	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], O, P, Q, R, S, T, U	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], O, P, Q, R, S, T, U	IPR023332	Proteasome alpha-type subunit	Family
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], O, P, Q, R, S, T, U	IPR001353	Proteasome, subunit alpha/beta	Family
A, C [auth B], D [auth C], E [auth D], F [auth E], A, C [auth B], D [auth C], E [auth D], F [auth E], G [auth F], H [auth G], O, P, Q, R, S, T, U	IPR019982	Proteasome alpha subunit, archaeal	Family
AA [auth a], B [auth H], BA [auth b], I, J, AA [auth a], B [auth H], BA [auth b], I, J, K, L, M, N, V, W, X, Y, Z	IPR023333	Proteasome B-type subunit	Family
AA [auth a], B [auth H], BA [auth b], I, J, AA [auth a], B [auth H], BA [auth b], I, J, K, L, M, N, V, W, X, Y, Z	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
AA [auth a], B [auth H], BA [auth b], I, J, AA [auth a], B [auth H], BA [auth b], I, J, K, L, M, N, V, W, X, Y, Z	IPR019983	Peptidase T1A, proteasome beta-subunit, archaeal	Family
AA [auth a], B [auth H], BA [auth b], I, J, AA [auth a], B [auth H], BA [auth b], I, J, K, L, M, N, V, W, X, Y, Z	IPR001353	Proteasome, subunit alpha/beta	Family
AA [auth a], B [auth H], BA [auth b], I, J, AA [auth a], B [auth H], BA [auth b], I, J, K, L, M, N, V, W, X, Y, Z	IPR000243	Peptidase T1A, proteasome beta-subunit	Family