Annotations: 2FHG

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	8085569	3000131	SCOP2B (2022-06-29)
AA [auth 1]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
C [auth B]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
E [auth D]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
G [auth F]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
M	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
O	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
Q	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
S	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
U	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
W	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
Y	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
B [auth H]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
BA [auth 2]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
L	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
P	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
R	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
T	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
V	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
Z	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
D [auth C]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
F [auth E]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
H [auth G]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
N	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	3000131	SCOP2B (2022-06-29)
X	SCOP2B Superfamily	Class II glutamine amidotransferases	8079171	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	e2fhgA1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
AA [auth 1]	Proteasome	e2fhg11	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
C [auth B]	Proteasome	e2fhgB1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
E [auth D]	Proteasome	e2fhgD1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
G [auth F]	Proteasome	e2fhgF1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
I	Proteasome	e2fhgI1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
K	Proteasome	e2fhgK1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
M	Proteasome	e2fhgM1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
O	Proteasome	e2fhgO1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Q	Proteasome	e2fhgQ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
S	Proteasome	e2fhgS1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
U	Proteasome	e2fhgU1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
W	Proteasome	e2fhgW1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Y	Proteasome	e2fhgY1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
B [auth H]	Proteasome	e2fhgH1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
BA [auth 2]	Proteasome	e2fhg21	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
J	Proteasome	e2fhgJ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
L	Proteasome	e2fhgL1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
P	Proteasome	e2fhgP1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
R	Proteasome	e2fhgR1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
T	Proteasome	e2fhgT1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
V	Proteasome	e2fhgV1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Z	Proteasome	e2fhgZ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
D [auth C]	Proteasome	e2fhgC1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
F [auth E]	Proteasome	e2fhgE1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
H [auth G]	Proteasome	e2fhgG1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
N	Proteasome	e2fhgN1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
X	Proteasome	e2fhgX1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
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)
AA [auth 1]	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 [auth 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)
E [auth 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)
G [auth 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)
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)
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)
O	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)
Q	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)
S	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)
U	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)
W	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)
Y	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)
B [auth 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)
BA [auth 2]	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)
P	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)
R	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)
T	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)
V	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)
Z	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 [auth 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 [auth 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)
H [auth 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)
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)
X	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, AA [auth 1], C [auth B], E [auth D], G [auth F], A, AA [auth 1], C [auth B], E [auth D], G [auth F], I, K, M, O, Q, S, U, W, Y	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
B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], J, L, N, P, R, T, V, X, 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, AA [auth 1], C [auth B], E [auth D], G [auth F], A, AA [auth 1], C [auth B], E [auth D], G [auth F], I, K, M, O, Q, S, U, W, Y	20S proteasome, alpha and beta subunits	peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity hydrolase activity catalytic activity endopeptidase activity threonine-type endopeptidase activity	catabolic process proteolysis involved in protein catabolic process proteasomal protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process proteolysis metabolic process cellular process protein metabolic process macromolecule metabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process catabolic process proteolysis involved in protein catabolic process proteasomal protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process proteolysis metabolic process cellular process protein metabolic process macromolecule metabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process ubiquitin-dependent protein catabolic process response to host defenses biological process involved in interspecies interaction between organisms response to stimulus response to other organism symbiont-mediated perturbation of host defenses response to defenses of other organism response to external stimulus response to biotic stimulus biological process involved in interaction with host biological process involved in symbiotic interaction response to host response to external biotic stimulus	protein-containing complex intracellular anatomical structure cellular anatomical structure proteasome core complex, alpha-subunit complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex cell periphery plasma membrane membrane external encapsulating structure protein-containing complex intracellular anatomical structure cellular anatomical structure proteasome core complex, alpha-subunit complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex cell periphery plasma membrane membrane external encapsulating structure cell wall peptidoglycan-based cell wall cytoplasm
B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], J, L, N, P, R, T, V, X, Z	proteasome, beta subunit	peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity hydrolase activity catalytic activity endopeptidase activity threonine-type endopeptidase activity protein binding binding enzyme binding zymogen binding	catabolic process proteolysis involved in protein catabolic process proteasomal protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process proteolysis metabolic process cellular process protein metabolic process macromolecule metabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process catabolic process proteolysis involved in protein catabolic process proteasomal protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process proteolysis metabolic process cellular process protein metabolic process macromolecule metabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process ubiquitin-dependent protein catabolic process response to host defenses biological process involved in interspecies interaction between organisms response to stimulus response to other organism symbiont-mediated perturbation of host defenses response to defenses of other organism response to external stimulus response to biotic stimulus biological process involved in interaction with host biological process involved in symbiotic interaction response to host response to external biotic stimulus	cellular anatomical structure extracellular region cell periphery plasma membrane membrane protein-containing complex intracellular anatomical structure catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex cellular anatomical structure extracellular region cell periphery plasma membrane membrane protein-containing complex intracellular anatomical structure catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, AA [auth 1], C [auth B], E [auth D], G [auth F], A, AA [auth 1], C [auth B], E [auth D], G [auth F], I, K, M, O, Q, S, U, W, Y	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A, AA [auth 1], C [auth B], E [auth D], G [auth F], A, AA [auth 1], C [auth B], E [auth D], G [auth F], I, K, M, O, Q, S, U, W, Y	IPR022296	Proteasome, alpha subunit, bacterial	Family
A, AA [auth 1], C [auth B], E [auth D], G [auth F], A, AA [auth 1], C [auth B], E [auth D], G [auth F], I, K, M, O, Q, S, U, W, Y	IPR050115	Proteasome subunit alpha	Family
A, AA [auth 1], C [auth B], E [auth D], G [auth F], A, AA [auth 1], C [auth B], E [auth D], G [auth F], I, K, M, O, Q, S, U, W, Y	IPR023332	Proteasome alpha-type subunit	Family
A, AA [auth 1], C [auth B], E [auth D], G [auth F], A, AA [auth 1], C [auth B], E [auth D], G [auth F], I, K, M, O, Q, S, U, W, Y	IPR001353	Proteasome, subunit alpha/beta	Family
B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], J, L, N, P, R, T, V, X, Z	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], J, L, N, P, R, T, V, X, Z	IPR023333	Proteasome B-type subunit	Family
B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], J, L, N, P, R, T, V, X, Z	IPR022483	Proteasome subunit beta, actinobacteria	Family
B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], B [auth H], BA [auth 2], D [auth C], F [auth E], H [auth G], J, L, N, P, R, T, V, X, Z	IPR001353	Proteasome, subunit alpha/beta	Family