3HF9

Crystal Structure of Mycobacterium Tuberculosis Proteasome open-gate mutant modified by inhibitor GL1

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	d3hf9a_	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	d3hf9b_	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 D]	d3hf9d_	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 F]	d3hf9f_	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 I]	d3hf9i_	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 K]	d3hf9k_	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 M]	d3hf9m_	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 O]	d3hf9o_	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 [auth Q]	d3hf9q_	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 [auth S]	d3hf9s_	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 [auth U]	d3hf9u_	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 [auth W]	d3hf9w_	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 [auth Y]	d3hf9y_	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 [auth 1]	d3hf91_	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 3]	d3hf93_	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)
CA [auth H]	d3hf9h_	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)
DA [auth C]	d3hf9c_	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)
DB [auth 4]	d3hf94_	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)
EA [auth E]	d3hf9e_	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)
FA [auth G]	d3hf9g_	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)
GA [auth J]	d3hf9j_	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)
HA [auth L]	d3hf9l_	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)
IA [auth N]	d3hf9n_	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)
JA [auth P]	d3hf9p_	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)
KA [auth R]	d3hf9r_	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)
LA [auth T]	d3hf9t_	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)
MA [auth V]	d3hf9v_	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)
NA [auth X]	d3hf9x_	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)
OA [auth Z]	d3hf9z_	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)
PA [auth 2]	d3hf92_	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 y]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
C [auth D]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
D [auth F]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
E [auth I]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
F [auth K]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
G [auth M]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
H [auth O]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
I [auth Q]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
J [auth S]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
K [auth U]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
L [auth W]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
M [auth Y]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
N [auth 1]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
O [auth a]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
P [auth b]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
Q [auth d]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
R [auth f]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
S [auth i]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
T [auth k]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
U [auth m]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
V [auth o]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
W [auth q]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
X [auth s]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
Y [auth u]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
Z [auth w]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	3000131	SCOP2B (2022-06-29)
BA [auth 3]	SCOP2B Superfamily	Class II glutamine amidotransferases	8085569	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	e3hf9A1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
AA [auth y]	Proteasome	e3hf9y1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
B	Proteasome	e3hf9B1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
C [auth D]	Proteasome	e3hf9D1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
D [auth F]	Proteasome	e3hf9F2	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
E [auth I]	Proteasome	e3hf9I1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
F [auth K]	Proteasome	e3hf9K1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
G [auth M]	Proteasome	e3hf9M1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
H [auth O]	Proteasome	e3hf9O1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
I [auth Q]	Proteasome	e3hf9Q1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
J [auth S]	Proteasome	e3hf9S1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
K [auth U]	Proteasome	e3hf9U1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
L [auth W]	Proteasome	e3hf9W3	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
M [auth Y]	Proteasome	e3hf9Y1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
N [auth 1]	Proteasome	e3hf911	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
O [auth a]	Proteasome	e3hf9a1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
P [auth b]	Proteasome	e3hf9b1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Q [auth d]	Proteasome	e3hf9d1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
R [auth f]	Proteasome	e3hf9f1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
S [auth i]	Proteasome	e3hf9i1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
T [auth k]	Proteasome	e3hf9k1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
U [auth m]	Proteasome	e3hf9m1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
V [auth o]	Proteasome	e3hf9o1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
W [auth q]	Proteasome	e3hf9q1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
X [auth s]	Proteasome	e3hf9s1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Y [auth u]	Proteasome	e3hf9u1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Z [auth w]	Proteasome	e3hf9w1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
BA [auth 3]	Proteasome	e3hf931	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
AB [auth v]	Proteasome	e3hf9v1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
BB [auth x]	Proteasome	e3hf9x1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
CA [auth H]	Proteasome	e3hf9H1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
CB [auth z]	Proteasome	e3hf9z1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
DA [auth C]	Proteasome	e3hf9C1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
DB [auth 4]	Proteasome	e3hf941	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
EA [auth E]	Proteasome	e3hf9E1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
FA [auth G]	Proteasome	e3hf9G1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
GA [auth J]	Proteasome	e3hf9J1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
HA [auth L]	Proteasome	e3hf9L1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
IA [auth N]	Proteasome	e3hf9N1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
JA [auth P]	Proteasome	e3hf9P1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
KA [auth R]	Proteasome	e3hf9R1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
LA [auth T]	Proteasome	e3hf9T1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
MA [auth V]	Proteasome	e3hf9V1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
NA [auth X]	Proteasome	e3hf9X1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
OA [auth Z]	Proteasome	e3hf9Z1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
PA [auth 2]	Proteasome	e3hf921	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
QA [auth h]	Proteasome	e3hf9h1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
RA [auth c]	Proteasome	e3hf9c1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
SA [auth e]	Proteasome	e3hf9e1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
TA [auth g]	Proteasome	e3hf9g1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
UA [auth j]	Proteasome	e3hf9j1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
VA [auth l]	Proteasome	e3hf9l1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
WA [auth n]	Proteasome	e3hf9n1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
XA [auth p]	Proteasome	e3hf9p1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
YA [auth r]	Proteasome	e3hf9r1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
ZA [auth t]	Proteasome	e3hf9t1	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 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	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 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)
D [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)
E [auth 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)
F [auth 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)
G [auth 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)
H [auth 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)
I [auth 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)
J [auth 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)
K [auth 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)
L [auth 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)
M [auth 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)
N [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)
O [auth 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)
P [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)
Q [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)
R [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)
S [auth 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)
T [auth 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)
U [auth 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)
V [auth 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)
W [auth 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)
X [auth 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)
Y [auth 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)
Z [auth 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)
BA [auth 3]	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)
AB [auth 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)
BB [auth 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)
CA [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)
CB [auth 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)
DA [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)
DB [auth 4]	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)
EA [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)
FA [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)
GA [auth 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)
HA [auth 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)
IA [auth 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)
JA [auth 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)
KA [auth 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)
LA [auth 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)
MA [auth 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)
NA [auth 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)
OA [auth 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)
PA [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)
QA [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)
RA [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)
SA [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)
TA [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)
UA [auth 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)
VA [auth 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)
WA [auth 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)
XA [auth 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)
YA [auth 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)
ZA [auth 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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, AA [auth y], B, BA [auth 3], C [auth D], A, AA [auth y], B, BA [auth 3], C [auth D], D [auth F], E [auth I], F [auth K], G [auth M], H [auth O], I [auth Q], J [auth S], K [auth U], L [auth W], M [auth Y], N [auth 1], O [auth a], P [auth b], Q [auth d], R [auth f], S [auth i], T [auth k], U [auth m], V [auth o], W [auth q], X [auth s], Y [auth u], Z [auth w]	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
AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], DB [auth 4], EA [auth E], FA [auth G], GA [auth J], HA [auth L], IA [auth N], JA [auth P], KA [auth R], LA [auth T], MA [auth V], NA [auth X], OA [auth Z], PA [auth 2], QA [auth h], RA [auth c], SA [auth e], TA [auth g], UA [auth j], VA [auth l], WA [auth n], XA [auth p], YA [auth r], ZA [auth t]	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 y], B, BA [auth 3], C [auth D], A, AA [auth y], B, BA [auth 3], C [auth D], D [auth F], E [auth I], F [auth K], G [auth M], H [auth O], I [auth Q], J [auth S], K [auth U], L [auth W], M [auth Y], N [auth 1], O [auth a], P [auth b], Q [auth d], R [auth f], S [auth i], T [auth k], U [auth m], V [auth o], W [auth q], X [auth s], Y [auth u], Z [auth w]	Proteasome (Alpha subunit) PrcA	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
AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], DB [auth 4], EA [auth E], FA [auth G], GA [auth J], HA [auth L], IA [auth N], JA [auth P], KA [auth R], LA [auth T], MA [auth V], NA [auth X], OA [auth Z], PA [auth 2], QA [auth h], RA [auth c], SA [auth e], TA [auth g], UA [auth j], VA [auth l], WA [auth n], XA [auth p], YA [auth r], ZA [auth t]	Proteasome (Beta subunit) PrcB	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

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, AA [auth y], B, BA [auth 3], C [auth D], A, AA [auth y], B, BA [auth 3], C [auth D], D [auth F], E [auth I], F [auth K], G [auth M], H [auth O], I [auth Q], J [auth S], K [auth U], L [auth W], M [auth Y], N [auth 1], O [auth a], P [auth b], Q [auth d], R [auth f], S [auth i], T [auth k], U [auth m], V [auth o], W [auth q], X [auth s], Y [auth u], Z [auth w]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A, AA [auth y], B, BA [auth 3], C [auth D], A, AA [auth y], B, BA [auth 3], C [auth D], D [auth F], E [auth I], F [auth K], G [auth M], H [auth O], I [auth Q], J [auth S], K [auth U], L [auth W], M [auth Y], N [auth 1], O [auth a], P [auth b], Q [auth d], R [auth f], S [auth i], T [auth k], U [auth m], V [auth o], W [auth q], X [auth s], Y [auth u], Z [auth w]	IPR022296	Proteasome, alpha subunit, bacterial	Family
A, AA [auth y], B, BA [auth 3], C [auth D], A, AA [auth y], B, BA [auth 3], C [auth D], D [auth F], E [auth I], F [auth K], G [auth M], H [auth O], I [auth Q], J [auth S], K [auth U], L [auth W], M [auth Y], N [auth 1], O [auth a], P [auth b], Q [auth d], R [auth f], S [auth i], T [auth k], U [auth m], V [auth o], W [auth q], X [auth s], Y [auth u], Z [auth w]	IPR050115	Proteasome subunit alpha	Family
A, AA [auth y], B, BA [auth 3], C [auth D], A, AA [auth y], B, BA [auth 3], C [auth D], D [auth F], E [auth I], F [auth K], G [auth M], H [auth O], I [auth Q], J [auth S], K [auth U], L [auth W], M [auth Y], N [auth 1], O [auth a], P [auth b], Q [auth d], R [auth f], S [auth i], T [auth k], U [auth m], V [auth o], W [auth q], X [auth s], Y [auth u], Z [auth w]	IPR023332	Proteasome alpha-type subunit	Family
A, AA [auth y], B, BA [auth 3], C [auth D], A, AA [auth y], B, BA [auth 3], C [auth D], D [auth F], E [auth I], F [auth K], G [auth M], H [auth O], I [auth Q], J [auth S], K [auth U], L [auth W], M [auth Y], N [auth 1], O [auth a], P [auth b], Q [auth d], R [auth f], S [auth i], T [auth k], U [auth m], V [auth o], W [auth q], X [auth s], Y [auth u], Z [auth w]	IPR001353	Proteasome, subunit alpha/beta	Family
AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], DB [auth 4], EA [auth E], FA [auth G], GA [auth J], HA [auth L], IA [auth N], JA [auth P], KA [auth R], LA [auth T], MA [auth V], NA [auth X], OA [auth Z], PA [auth 2], QA [auth h], RA [auth c], SA [auth e], TA [auth g], UA [auth j], VA [auth l], WA [auth n], XA [auth p], YA [auth r], ZA [auth t]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], DB [auth 4], EA [auth E], FA [auth G], GA [auth J], HA [auth L], IA [auth N], JA [auth P], KA [auth R], LA [auth T], MA [auth V], NA [auth X], OA [auth Z], PA [auth 2], QA [auth h], RA [auth c], SA [auth e], TA [auth g], UA [auth j], VA [auth l], WA [auth n], XA [auth p], YA [auth r], ZA [auth t]	IPR022296	Proteasome, alpha subunit, bacterial	Family
AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], DB [auth 4], EA [auth E], FA [auth G], GA [auth J], HA [auth L], IA [auth N], JA [auth P], KA [auth R], LA [auth T], MA [auth V], NA [auth X], OA [auth Z], PA [auth 2], QA [auth h], RA [auth c], SA [auth e], TA [auth g], UA [auth j], VA [auth l], WA [auth n], XA [auth p], YA [auth r], ZA [auth t]	IPR050115	Proteasome subunit alpha	Family
AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], DB [auth 4], EA [auth E], FA [auth G], GA [auth J], HA [auth L], IA [auth N], JA [auth P], KA [auth R], LA [auth T], MA [auth V], NA [auth X], OA [auth Z], PA [auth 2], QA [auth h], RA [auth c], SA [auth e], TA [auth g], UA [auth j], VA [auth l], WA [auth n], XA [auth p], YA [auth r], ZA [auth t]	IPR023332	Proteasome alpha-type subunit	Family
AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], AB [auth v], BB [auth x], CA [auth H], CB [auth z], DA [auth C], DB [auth 4], EA [auth E], FA [auth G], GA [auth J], HA [auth L], IA [auth N], JA [auth P], KA [auth R], LA [auth T], MA [auth V], NA [auth X], OA [auth Z], PA [auth 2], QA [auth h], RA [auth c], SA [auth e], TA [auth g], UA [auth j], VA [auth l], WA [auth n], XA [auth p], YA [auth r], ZA [auth t]	IPR001353	Proteasome, subunit alpha/beta	Family