6UTF

Allosteric coupling between alpha-rings of the 20S proteasome, archaea 20S proteasome singly capped with a PAN complex

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth M]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
D [auth N]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
F [auth H]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
G [auth V]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
H [auth I]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
A [auth Z]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
C [auth 1]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
E [auth 2]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
I [auth W]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
K [auth X]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
L [auth K]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
M [auth Y]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
N [auth L]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
P [auth B]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
U [auth G]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
O [auth A]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
Q [auth C]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
R [auth D]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
S [auth E]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
T [auth F]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
AA [auth T]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
BA [auth U]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
X [auth Q]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
V [auth O]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
W [auth P]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
Y [auth R]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
Z [auth S]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	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 [auth M]	Proteasome	e6utfM1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
D [auth N]	Proteasome	e6utfN1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
F [auth H]	Proteasome	e6utfH1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
G [auth V]	Proteasome	e6utfV1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
H [auth I]	Proteasome	e6utfI1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
A [auth Z]	Proteasome	e6utfZ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
C [auth 1]	Proteasome	e6utf11	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
E [auth 2]	Proteasome	e6utf21	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
I [auth W]	Proteasome	e6utfW1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
J	Proteasome	e6utfJ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
K [auth X]	Proteasome	e6utfX1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
L [auth K]	Proteasome	e6utfK1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
M [auth Y]	Proteasome	e6utfY1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
N [auth L]	Proteasome	e6utfL1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
P [auth B]	Proteasome	e6utfB1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
U [auth G]	Proteasome	e6utfG1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
O [auth A]	Proteasome	e6utfA1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Q [auth C]	Proteasome	e6utfC1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
R [auth D]	Proteasome	e6utfD1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
S [auth E]	Proteasome	e6utfE1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
T [auth F]	Proteasome	e6utfF1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
AA [auth T]	Proteasome	e6utfT1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
BA [auth U]	Proteasome	e6utfU1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
X [auth Q]	Proteasome	e6utfQ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
V [auth O]	Proteasome	e6utfO1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
W [auth P]	Proteasome	e6utfP1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Y [auth R]	Proteasome	e6utfR1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Z [auth S]	Proteasome	e6utfS1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], F [auth H], G [auth V], H [auth I], I [auth W], J, K [auth X], L [auth K], M [auth Y], N [auth L]	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
O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], T [auth F], U [auth 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
O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], T [auth F], U [auth G]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], Y [auth R], Z [auth S]	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
AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], Y [auth R], Z [auth S]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], F [auth H], G [auth V], H [auth I], I [auth W], J, K [auth X], L [auth K], M [auth Y], N [auth L]	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
O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], T [auth F], U [auth G]	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 T], BA [auth U], V [auth O], W [auth P], X [auth Q], AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], Y [auth R], Z [auth S]	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

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], F [auth H], G [auth V], H [auth I], I [auth W], J, K [auth X], L [auth K], M [auth Y], N [auth L]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], F [auth H], G [auth V], H [auth I], I [auth W], J, K [auth X], L [auth K], M [auth Y], N [auth L]	IPR023333	Proteasome B-type subunit	Family
A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], F [auth H], G [auth V], H [auth I], I [auth W], J, K [auth X], L [auth K], M [auth Y], N [auth L]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], F [auth H], G [auth V], H [auth I], I [auth W], J, K [auth X], L [auth K], M [auth Y], N [auth L]	IPR019983	Peptidase T1A, proteasome beta-subunit, archaeal	Family
A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], F [auth H], G [auth V], H [auth I], I [auth W], J, K [auth X], L [auth K], M [auth Y], N [auth L]	IPR001353	Proteasome, subunit alpha/beta	Family
A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], A [auth Z], B [auth M], C [auth 1], D [auth N], E [auth 2], F [auth H], G [auth V], H [auth I], I [auth W], J, K [auth X], L [auth K], M [auth Y], N [auth L]	IPR000243	Peptidase T1A, proteasome beta-subunit	Family
O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], T [auth F], U [auth G]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], T [auth F], U [auth G]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], T [auth F], U [auth G]	IPR023332	Proteasome alpha-type subunit	Family
O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], T [auth F], U [auth G]	IPR001353	Proteasome, subunit alpha/beta	Family
O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], O [auth A], P [auth B], Q [auth C], R [auth D], S [auth E], T [auth F], U [auth G]	IPR019982	Proteasome alpha subunit, archaeal	Family
AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], Y [auth R], Z [auth S]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], Y [auth R], Z [auth S]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], Y [auth R], Z [auth S]	IPR023332	Proteasome alpha-type subunit	Family
AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], Y [auth R], Z [auth S]	IPR001353	Proteasome, subunit alpha/beta	Family
AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], AA [auth T], BA [auth U], V [auth O], W [auth P], X [auth Q], Y [auth R], Z [auth S]	IPR019982	Proteasome alpha subunit, archaeal	Family

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6UTF

Allosteric coupling between alpha-rings of the 20S proteasome, archaea 20S proteasome singly capped with a PAN complex

External Resource: Annotation

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Domain Annotation: ECOD Classification ECOD Database Homepage

Protein Family Annotation Pfam Database Homepage

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

InterPro: Protein Family Classification InterPro Database Homepage