2FHH

Crystal Structure of Mycobacterium Tuberculosis Proteasome in complex with a peptidyl boronate inhibitor MLN-273

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2fhha_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
AA [auth 1]	d2fhh1_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
C [auth B]	d2fhhb_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
E [auth D]	d2fhhd_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
G [auth F]	d2fhhf_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
I	d2fhhi_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
K	d2fhhk_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
M	d2fhhm_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
O	d2fhho_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
Q	d2fhhq_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
S	d2fhhs_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
U	d2fhhu_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
W	d2fhhw_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
Y	d2fhhy_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
B [auth H]	d2fhhh_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
BA [auth 2]	d2fhh2_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
D [auth C]	d2fhhc_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
F [auth E]	d2fhhe_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
H [auth G]	d2fhhg_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
J	d2fhhj_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
L	d2fhhl_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
N	d2fhhn_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
P	d2fhhp_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
R	d2fhhr_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
T	d2fhht_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
V	d2fhhv_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
X	d2fhhx_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
Z	d2fhhz_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)

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)
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)
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)
N	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)
X	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)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Proteasome	e2fhhA1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
AA [auth 1]	Proteasome	e2fhh11	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
C [auth B]	Proteasome	e2fhhB1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
E [auth D]	Proteasome	e2fhhD1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
G [auth F]	Proteasome	e2fhhF1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
I	Proteasome	e2fhhI1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
K	Proteasome	e2fhhK1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
M	Proteasome	e2fhhM1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
O	Proteasome	e2fhhO1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Q	Proteasome	e2fhhQ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
S	Proteasome	e2fhhS1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
U	Proteasome	e2fhhU1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
W	Proteasome	e2fhhW1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Y	Proteasome	e2fhhY1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
B [auth H]	Proteasome	e2fhhH1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
BA [auth 2]	Proteasome	e2fhh21	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
D [auth C]	Proteasome	e2fhhC1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
F [auth E]	Proteasome	e2fhhE1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
H [auth G]	Proteasome	e2fhhG1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
J	Proteasome	e2fhhJ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
L	Proteasome	e2fhhL1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
N	Proteasome	e2fhhN1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
P	Proteasome	e2fhhP1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
R	Proteasome	e2fhhR1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
T	Proteasome	e2fhhT1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
V	Proteasome	e2fhhV1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
X	Proteasome	e2fhhX1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Z	Proteasome	e2fhhZ1	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)
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)
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)
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)
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)
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)
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)

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	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 organonitrogen compound catabolic process organonitrogen compound metabolic 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 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 modification-dependent macromolecule catabolic process modification-dependent protein catabolic process	protein-containing complex intracellular anatomical structure proteasome core complex, alpha-subunit complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex cellular anatomical entity intracellular protein-containing complex cell periphery plasma membrane membrane external encapsulating structure protein-containing complex intracellular anatomical structure proteasome core complex, alpha-subunit complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex cellular anatomical entity 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	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 organonitrogen compound catabolic process organonitrogen compound metabolic 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 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 modification-dependent macromolecule catabolic process modification-dependent protein catabolic process	extracellular region cellular anatomical entity 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 extracellular region cellular anatomical entity 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	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