6UTI

Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome with singly capped 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)
A	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
H [auth O]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
I [auth P]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
J [auth Q]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
K [auth R]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
L [auth S]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
M [auth T]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
N [auth U]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034248	3000131	SCOP2B (2022-06-29)
AA [auth a]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
BA [auth b]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
O [auth H]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
P [auth I]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
Q [auth J]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
R [auth K]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
S [auth L]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
T [auth M]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
U [auth N]	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
V	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
W	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
X	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
Y	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	3000131	SCOP2B (2022-06-29)
Z	SCOP2B Superfamily	Class II glutamine amidotransferases	8034254	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	Proteasome	e6utiA1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
B	Proteasome	e6utiB1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
C	Proteasome	e6utiC1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
D	Proteasome	e6utiD1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
E	Proteasome	e6utiE1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
F	Proteasome	e6utiF1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
G	Proteasome	e6utiG1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
H [auth O]	Proteasome	e6utiO1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
I [auth P]	Proteasome	e6utiP1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
J [auth Q]	Proteasome	e6utiQ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
K [auth R]	Proteasome	e6utiR1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
L [auth S]	Proteasome	e6utiS1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
M [auth T]	Proteasome	e6utiT1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
N [auth U]	Proteasome	e6utiU1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
AA [auth a]	Proteasome	e6utia1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
BA [auth b]	Proteasome	e6utib1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
O [auth H]	Proteasome	e6utiH1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
P [auth I]	Proteasome	e6utiI1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Q [auth J]	Proteasome	e6utiJ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
R [auth K]	Proteasome	e6utiK1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
S [auth L]	Proteasome	e6utiL1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
T [auth M]	Proteasome	e6utiM1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
U [auth N]	Proteasome	e6utiN1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
V	Proteasome	e6utiV1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
W	Proteasome	e6utiW1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
X	Proteasome	e6utiX1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Y	Proteasome	e6utiY1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Z	Proteasome	e6utiZ1	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, 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
A, B, C, D, E A, B, C, D, E, F, G	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], M [auth T], N [auth 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
H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], M [auth T], N [auth U]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], R [auth K], S [auth L], T [auth M], U [auth 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, B, C, D, E A, B, C, D, E, F, 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
H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], M [auth T], N [auth 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], BA [auth b], O [auth H], P [auth I], Q [auth J], AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], R [auth K], S [auth L], T [auth M], U [auth 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, B, C, D, E A, B, C, D, E, F, G	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
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	IPR023332	Proteasome alpha-type subunit	Family
A, B, C, D, E A, B, C, D, E, F, G	IPR001353	Proteasome, subunit alpha/beta	Family
A, B, C, D, E A, B, C, D, E, F, G	IPR019982	Proteasome alpha subunit, archaeal	Family
H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], M [auth T], N [auth U]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], M [auth T], N [auth U]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], M [auth T], N [auth U]	IPR023332	Proteasome alpha-type subunit	Family
H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], M [auth T], N [auth U]	IPR001353	Proteasome, subunit alpha/beta	Family
H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], H [auth O], I [auth P], J [auth Q], K [auth R], L [auth S], M [auth T], N [auth U]	IPR019982	Proteasome alpha subunit, archaeal	Family
AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], R [auth K], S [auth L], T [auth M], U [auth N], V, W, X, Y, Z	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], R [auth K], S [auth L], T [auth M], U [auth N], V, W, X, Y, Z	IPR023333	Proteasome B-type subunit	Family
AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], R [auth K], S [auth L], T [auth M], U [auth N], V, W, X, Y, Z	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], R [auth K], S [auth L], T [auth M], U [auth N], V, W, X, Y, Z	IPR019983	Peptidase T1A, proteasome beta-subunit, archaeal	Family
AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], R [auth K], S [auth L], T [auth M], U [auth N], V, W, X, Y, Z	IPR001353	Proteasome, subunit alpha/beta	Family
AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], AA [auth a], BA [auth b], O [auth H], P [auth I], Q [auth J], R [auth K], S [auth L], T [auth M], U [auth N], V, W, X, Y, Z	IPR000243	Peptidase T1A, proteasome beta-subunit	Family