3UNB

Mouse constitutive 20S proteasome in complex with PR-957

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	d3unba_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
CA [auth c]	d3unbc_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
O	d3unbo_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
QA [auth q]	d3unbq_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
R	d3unbr_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
D	d3unbd_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
E	d3unbe_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	automated matches	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
S	d3unbs_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	automated matches	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
F	d3unbf_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
T	d3unbt_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
G	d3unbg_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
U	d3unbu_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	Proteasome alpha subunit (non-catalytic)	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
H	d3unbh_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
V	d3unbv_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
I	d3unbi_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
W	d3unbw_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
AB [auth 1]	d3unb1_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
K	d3unbk_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
Y	d3unby_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
CB [auth 3]	d3unb3_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
M	d3unbm_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
BA [auth b]	d3unbb_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
DB [auth 4]	d3unb4_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
N	d3unbn_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
PA [auth p]	d3unbp_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
J	d3unbj_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
X	d3unbx_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
BB [auth 2]	d3unb2_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
L	d3unbl_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
Z	d3unbz_	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	Proteasome subunits	automated matches	(Mus musculus ) [TaxId: 10090 ],	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	8064016	3000131	SCOP2B (2022-06-29)
CA [auth c]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064016	3000131	SCOP2B (2022-06-29)
O	SCOP2B Superfamily	Class II glutamine amidotransferases	8064016	3000131	SCOP2B (2022-06-29)
QA [auth q]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064016	3000131	SCOP2B (2022-06-29)
B	SCOP2 Family	Proteasome subunits	8064041	4002254	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Class II glutamine amidotransferases	8064042	3000131	SCOP2 (2022-06-29)
DA [auth d]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064042	3000131	SCOP2B (2022-06-29)
P	SCOP2B Superfamily	Class II glutamine amidotransferases	8064042	3000131	SCOP2B (2022-06-29)
RA [auth r]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064042	3000131	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Class II glutamine amidotransferases	8064006	3000131	SCOP2B (2022-06-29)
EA [auth e]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064006	3000131	SCOP2B (2022-06-29)
Q	SCOP2B Superfamily	Class II glutamine amidotransferases	8064006	3000131	SCOP2B (2022-06-29)
SA [auth s]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064006	3000131	SCOP2B (2022-06-29)
FA [auth f]	SCOP2B Superfamily	Class II glutamine amidotransferases	8100760	3000131	SCOP2B (2022-06-29)
R	SCOP2B Superfamily	Class II glutamine amidotransferases	8100760	3000131	SCOP2B (2022-06-29)
TA [auth t]	SCOP2B Superfamily	Class II glutamine amidotransferases	8100760	3000131	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Class II glutamine amidotransferases	8100760	3000131	SCOP2B (2022-06-29)
E	SCOP2 Family	Proteasome subunits	8064057	4002254	SCOP2 (2022-06-29)
E	SCOP2 Superfamily	Class II glutamine amidotransferases	8064058	3000131	SCOP2 (2022-06-29)
GA [auth g]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064058	3000131	SCOP2B (2022-06-29)
S	SCOP2B Superfamily	Class II glutamine amidotransferases	8064058	3000131	SCOP2B (2022-06-29)
UA [auth u]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064058	3000131	SCOP2B (2022-06-29)
F	SCOP2 Family	Proteasome subunits	8064055	4002254	SCOP2 (2022-06-29)
F	SCOP2 Superfamily	Class II glutamine amidotransferases	8064056	3000131	SCOP2 (2022-06-29)
HA [auth h]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064056	3000131	SCOP2B (2022-06-29)
T	SCOP2B Superfamily	Class II glutamine amidotransferases	8064056	3000131	SCOP2B (2022-06-29)
VA [auth v]	SCOP2B Superfamily	Class II glutamine amidotransferases	8064056	3000131	SCOP2B (2022-06-29)
H	SCOP2 Family	Proteasome subunits	8079519	4002254	SCOP2 (2022-06-29)
H	SCOP2 Superfamily	Class II glutamine amidotransferases	8079520	3000131	SCOP2 (2022-06-29)
JA [auth j]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079520	3000131	SCOP2B (2022-06-29)
V	SCOP2B Superfamily	Class II glutamine amidotransferases	8079520	3000131	SCOP2B (2022-06-29)
XA [auth x]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079520	3000131	SCOP2B (2022-06-29)
AB [auth 1]	SCOP2 Family	Proteasome subunits	8079493	4002254	SCOP2 (2022-06-29)
AB [auth 1]	SCOP2 Superfamily	Class II glutamine amidotransferases	8079494	3000131	SCOP2 (2022-06-29)
K	SCOP2B Superfamily	Class II glutamine amidotransferases	8079494	3000131	SCOP2B (2022-06-29)
MA [auth m]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079494	3000131	SCOP2B (2022-06-29)
Y	SCOP2B Superfamily	Class II glutamine amidotransferases	8079494	3000131	SCOP2B (2022-06-29)
BA [auth b]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079528	3000131	SCOP2B (2022-06-29)
DB [auth 4]	SCOP2 Family	Proteasome subunits	8079527	4002254	SCOP2 (2022-06-29)
DB [auth 4]	SCOP2 Superfamily	Class II glutamine amidotransferases	8079528	3000131	SCOP2 (2022-06-29)
N	SCOP2B Superfamily	Class II glutamine amidotransferases	8079528	3000131	SCOP2B (2022-06-29)
PA [auth p]	SCOP2B Superfamily	Class II glutamine amidotransferases	8079528	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	e3unbA1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
CA [auth c]	Proteasome	e3unbc1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
O	Proteasome	e3unbO1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
QA [auth q]	Proteasome	e3unbq1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
B	Proteasome	e3unbB1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
DA [auth d]	Proteasome	e3unbd1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
P	Proteasome	e3unbP1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
RA [auth r]	Proteasome	e3unbr1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
C	Proteasome	e3unbC1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
EA [auth e]	Proteasome	e3unbe1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Q	Proteasome	e3unbQ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
SA [auth s]	Proteasome	e3unbs1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
FA [auth f]	Proteasome	e3unbf1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
R	Proteasome	e3unbR1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
TA [auth t]	Proteasome	e3unbt1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
D	Proteasome	e3unbD1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
E	Proteasome	e3unbE1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
GA [auth g]	Proteasome	e3unbg1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
S	Proteasome	e3unbS1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
UA [auth u]	Proteasome	e3unbu1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
F	Proteasome	e3unbF1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
HA [auth h]	Proteasome	e3unbh1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
T	Proteasome	e3unbT1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
VA [auth v]	Proteasome	e3unbv1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
G	Proteasome	e3unbG1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
IA [auth i]	Proteasome	e3unbi1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
U	Proteasome	e3unbU1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
WA [auth w]	Proteasome	e3unbw1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
H	Proteasome	e3unbH1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
JA [auth j]	Proteasome	e3unbj1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
V	Proteasome	e3unbV1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
XA [auth x]	Proteasome	e3unbx1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
I	Proteasome	e3unbI1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
W	Proteasome	e3unbW1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
YA [auth y]	Proteasome	e3unby1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
KA [auth k]	Proteasome	e3unbk1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
AB [auth 1]	Proteasome	e3unb11	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
K	Proteasome	e3unbK1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
MA [auth m]	Proteasome	e3unbm1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Y	Proteasome	e3unbY1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
AA [auth a]	Proteasome	e3unba1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
CB [auth 3]	Proteasome	e3unb31	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
OA [auth o]	Proteasome	e3unbo1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
M	Proteasome	e3unbM1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
BA [auth b]	Proteasome	e3unbb1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
DB [auth 4]	Proteasome	e3unb41	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
N	Proteasome	e3unbN1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
PA [auth p]	Proteasome	e3unbp1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
J	Proteasome	e3unbJ1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
LA [auth l]	Proteasome	e3unbl1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
X	Proteasome	e3unbX1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
ZA [auth z]	Proteasome	e3unbz1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
BB [auth 2]	Proteasome	e3unb21	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
L	Proteasome	e3unbL1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
NA [auth n]	Proteasome	e3unbn1	A: a+b four layers	X: Ntn/PP2C	H: Ntn	T: Proteasome subunits	F: Proteasome	ECOD (1.6)
Z	Proteasome	e3unbZ1	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)
CA [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)
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)
QA [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)
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)
DA [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)
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)
RA [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)
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)
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)
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)
SA [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)
FA [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)
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)
TA [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)
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)
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)
GA [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)
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)
UA [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)
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)
HA [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)
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)
VA [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)
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)
IA [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)
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)
WA [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)
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)
JA [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)
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)
XA [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)
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)
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)
YA [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)
KA [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)
AB [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)
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)
MA [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)
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)
AA [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)
CB [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)
OA [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)
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)
BA [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)
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)
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)
PA [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)
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)
LA [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)
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)
ZA [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)
BB [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)
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)
NA [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)
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, CA [auth c], O, QA [auth q]	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, CA [auth c], O, QA [auth q]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
B, DA [auth d], P, RA [auth r]	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, DA [auth d], P, RA [auth r]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
C, EA [auth e], Q, SA [auth s]	PF00227	Proteasome subunit (Proteasome)	Proteasome subunit	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...	The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].	Domain
C, EA [auth e], Q, SA [auth s]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
D, FA [auth f], R, TA [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
D, FA [auth f], R, TA [auth t]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
E, GA [auth g], S, UA [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
E, GA [auth g], S, UA [auth u]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
F, HA [auth h], T, VA [auth v]	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
F, HA [auth h], T, VA [auth v]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
G, IA [auth i], U, WA [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
G, IA [auth i], U, WA [auth w]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
H, JA [auth j], V, XA [auth x]	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, JA [auth j], V, XA [auth x]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
H, JA [auth j], V, XA [auth x]	PF12465	Proteasome beta subunits C terminal (Pr_beta_C)	Proteasome beta subunits C terminal	-	Family
I, KA [auth k], W, YA [auth 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
I, KA [auth k], W, YA [auth y]	PF10584	Proteasome subunit A N-terminal signature (Proteasome_A_N)	Proteasome subunit A N-terminal signature	-	Family
AB [auth 1], K, MA [auth m], 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
AA [auth a], CB [auth 3], M, OA [auth o]	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
BA [auth b], DB [auth 4], N, PA [auth p]	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
J, LA [auth l], X, ZA [auth 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
J, LA [auth l], X, ZA [auth z]	PF12465	Proteasome beta subunits C terminal (Pr_beta_C)	Proteasome beta subunits C terminal	-	Family
BB [auth 2], L, NA [auth n], 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, CA [auth c], O, QA [auth q]	Proteasome subunit alpha type-2	-	biological process involved in interspecies interaction between organisms response to stimulus response to other organism response to external stimulus response to external biotic stimulus response to virus response to biotic stimulus catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process biological process involved in interspecies interaction between organisms response to stimulus response to other organism response to external stimulus response to external biotic stimulus response to virus response to biotic stimulus catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cytoplasmic ribonucleoprotein granule intracellular membraneless organelle ribonucleoprotein granule intracellular organelle organelle membraneless organelle supramolecular complex P-body protein-containing complex catalytic complex cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cytoplasmic ribonucleoprotein granule intracellular membraneless organelle ribonucleoprotein granule intracellular organelle organelle membraneless organelle supramolecular complex P-body protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, alpha-subunit complex membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
B, DA [auth d], P, RA [auth r]	Proteasome subunit alpha type-4	-	catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cytoplasmic ribonucleoprotein granule intracellular membraneless organelle ribonucleoprotein granule intracellular organelle organelle membraneless organelle supramolecular complex P-body protein-containing complex catalytic complex cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cytoplasmic ribonucleoprotein granule intracellular membraneless organelle ribonucleoprotein granule intracellular organelle organelle membraneless organelle supramolecular complex P-body protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, alpha-subunit complex membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
C, EA [auth e], Q, SA [auth s]	Proteasome subunit alpha type-7	identical protein binding protein binding binding	catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, alpha-subunit complex membrane-bounded organelle nucleus cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, alpha-subunit complex membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen
D, FA [auth f], R, TA [auth t]	Proteasome subunit alpha type-5	-	catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process protein metabolic process catabolic process proteolysis involved in protein catabolic process primary metabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, alpha-subunit complex membrane-bounded organelle nucleus cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, alpha-subunit complex membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen
E, GA [auth g], S, UA [auth u]	Proteasome subunit alpha type-1	binding lipid binding lipopolysaccharide binding carbohydrate derivative binding	immune system process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process immune system process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process regulation of defense response response to stimulus regulation of response to external stimulus negative regulation of inflammatory response negative regulation of biological process inflammatory response to antigenic stimulus response to stress regulation of response to stress regulation of immune system process negative regulation of inflammatory response to antigenic stimulus regulation of biological process defense response immune response negative regulation of response to stimulus negative regulation of immune response regulation of inflammatory response to antigenic stimulus biological regulation response to external stimulus regulation of inflammatory response regulation of response to stimulus negative regulation of immune system process negative regulation of response to external stimulus negative regulation of defense response regulation of immune response inflammatory response	protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex intracellular anatomical structure cellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex intracellular organelle centrosome microtubule organizing center cytoskeleton protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex intracellular protein-containing complex intracellular anatomical structure cellular anatomical structure proteasome core complex, alpha-subunit complex proteasome core complex intracellular organelle centrosome microtubule organizing center cytoskeleton organelle membraneless organelle intracellular membraneless organelle microtubule cytoskeleton cytoplasm cytosol membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
F, HA [auth h], T, VA [auth v]	Proteasome subunit alpha type-3	ubiquitin protein ligase binding protein binding binding ubiquitin-like protein ligase binding enzyme binding	catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process regulation of biological process catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process regulation of biological process regulation of cellular process regulation of catalytic activity regulation of protein metabolic process regulation of peptidase activity biological regulation regulation of macromolecule metabolic process regulation of primary metabolic process regulation of molecular function regulation of proteolysis regulation of hydrolase activity regulation of endopeptidase activity regulation of metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, alpha-subunit complex membrane-bounded organelle nucleus cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, alpha-subunit complex membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen
G, IA [auth i], U, WA [auth w]	Proteasome subunit alpha type-6	transcription factor binding RNA polymerase II-specific DNA-binding transcription factor binding protein binding binding DNA-binding transcription factor binding NF-kappaB binding RNA binding organic cyclic compound binding nucleic acid binding	catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process positive regulation of DNA-binding transcription factor activity catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process positive regulation of DNA-binding transcription factor activity regulation of cellular process positive regulation of NF-kappaB transcription factor activity RNA metabolic process regulation of primary metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process positive regulation of molecular function nucleic acid biosynthetic process DNA-templated transcription regulation of RNA metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of biosynthetic process regulation of biological process biological regulation regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process regulation of molecular function regulation of gene expression biosynthetic process regulation of DNA-binding transcription factor activity regulation of macromolecule biosynthetic process regulation of DNA-templated transcription regulation of metabolic process developmental process muscle structure development skeletal muscle organ development skeletal muscle tissue development anatomical structure development animal organ development muscle tissue development muscle organ development tissue development striated muscle tissue development	membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle cellular anatomical structure organelle lumen organelle nuclear periphery nuclear lumen nuclear matrix intracellular membraneless organelle membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle cellular anatomical structure organelle lumen organelle nuclear periphery nuclear lumen nuclear matrix intracellular membraneless organelle sarcomere membraneless organelle contractile muscle fiber cytoplasm supramolecular fiber myofibril supramolecular polymer supramolecular complex protein-containing complex proteasome core complex, alpha-subunit complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex cytosol cytoplasmic ribonucleoprotein granule ribonucleoprotein granule P-body nucleoplasm ribosome
H, JA [auth j], V, XA [auth x]	Proteasome subunit beta type-7	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 proteolysis metabolic process cellular process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex membrane-bounded organelle nucleus cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nuclear body intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen
I, KA [auth k], W, YA [auth y]	Proteasome subunit beta type-3	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity endopeptidase activity	catabolic process metabolic process cellular process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process proteolysis involved in protein catabolic process proteasomal protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis catabolic process metabolic process cellular process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process proteolysis involved in protein catabolic process proteasomal protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process proteolysis ubiquitin-dependent protein catabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex membrane-bounded organelle nucleus cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen
AB [auth 1], K, MA [auth m], Y	Proteasome subunit beta type-5	peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity hydrolase activity catalytic activity endopeptidase activity threonine-type endopeptidase activity	response to oxidative stress response to stimulus response to stress proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process catabolic process proteolysis involved in protein catabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process response to oxidative stress response to stimulus response to stress proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process catabolic process proteolysis involved in protein catabolic process proteasomal protein catabolic process protein catabolic process proteasome-mediated ubiquitin-dependent protein catabolic process macromolecule catabolic process modification-dependent macromolecule catabolic process modification-dependent protein catabolic process ubiquitin-dependent protein catabolic process	intracellular organelle centrosome microtubule organizing center cellular anatomical structure intracellular anatomical structure cytoskeleton organelle membraneless organelle intracellular membraneless organelle microtubule cytoskeleton cytoplasm cytosol protein-containing complex catalytic complex intracellular organelle centrosome microtubule organizing center cellular anatomical structure intracellular anatomical structure cytoskeleton organelle membraneless organelle intracellular membraneless organelle microtubule cytoskeleton cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
AA [auth a], CB [auth 3], M, OA [auth o]	Proteasome subunit beta type-4	binding lipid binding lipopolysaccharide binding carbohydrate derivative binding	regulation of defense response response to stimulus regulation of response to external stimulus negative regulation of inflammatory response negative regulation of biological process inflammatory response to antigenic stimulus response to stress regulation of response to stress regulation of immune system process negative regulation of inflammatory response to antigenic stimulus regulation of biological process defense response immune response negative regulation of response to stimulus regulation of defense response response to stimulus regulation of response to external stimulus negative regulation of inflammatory response negative regulation of biological process inflammatory response to antigenic stimulus response to stress regulation of response to stress regulation of immune system process negative regulation of inflammatory response to antigenic stimulus regulation of biological process defense response immune response negative regulation of response to stimulus negative regulation of immune response regulation of inflammatory response to antigenic stimulus biological regulation response to external stimulus regulation of inflammatory response regulation of response to stimulus negative regulation of immune system process immune system process negative regulation of response to external stimulus negative regulation of defense response regulation of immune response inflammatory response catabolic process proteolysis involved in protein catabolic process proteolysis metabolic process cellular process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex nucleus membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen intracellular membraneless organelle cilium plasma membrane bounded cell projection ciliary basal body cell projection microtubule organizing center cytoskeleton membraneless organelle microtubule cytoskeleton
BA [auth b], DB [auth 4], N, PA [auth p]	Proteasome subunit beta type-6	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 proteolysis metabolic process cellular process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle mitochondrion organelle intracellular membrane-bounded organelle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle mitochondrion organelle intracellular membrane-bounded organelle protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex nucleus membrane-enclosed lumen intracellular organelle lumen nucleoplasm organelle lumen nuclear lumen
J, LA [auth l], X, ZA [auth z]	Proteasome subunit beta type-2	-	response to stimulus response to chemical response to organic cyclic compound 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	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex membrane-bounded organelle nucleus cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen
BB [auth 2], L, NA [auth n], Z	Proteasome subunit beta type-1	-	catabolic process proteolysis involved in protein catabolic process proteolysis metabolic process cellular process primary metabolic process protein catabolic process protein metabolic process macromolecule metabolic process macromolecule catabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex membrane-bounded organelle nucleus cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex peptidase complex proteasome complex endopeptidase complex proteasome core complex intracellular protein-containing complex proteasome core complex, beta-subunit complex membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, CA [auth c], O, QA [auth q]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
A, CA [auth c], O, QA [auth q]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A, CA [auth c], O, QA [auth q]	IPR050115	Proteasome subunit alpha	Family
A, CA [auth c], O, QA [auth q]	IPR023332	Proteasome alpha-type subunit	Family
A, CA [auth c], O, QA [auth q]	IPR001353	Proteasome, subunit alpha/beta	Family
B, DA [auth d], P, RA [auth r]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
B, DA [auth d], P, RA [auth r]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
B, DA [auth d], P, RA [auth r]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
B, DA [auth d], P, RA [auth r]	IPR050115	Proteasome subunit alpha	Family
B, DA [auth d], P, RA [auth r]	IPR023332	Proteasome alpha-type subunit	Family
B, DA [auth d], P, RA [auth r]	IPR001353	Proteasome, subunit alpha/beta	Family
C, EA [auth e], Q, SA [auth s]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
C, EA [auth e], Q, SA [auth s]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
C, EA [auth e], Q, SA [auth s]	IPR050115	Proteasome subunit alpha	Family
C, EA [auth e], Q, SA [auth s]	IPR023332	Proteasome alpha-type subunit	Family
C, EA [auth e], Q, SA [auth s]	IPR001353	Proteasome, subunit alpha/beta	Family
D, FA [auth f], R, TA [auth t]	IPR033812	Proteasome subunit alpha5	Family
D, FA [auth f], R, TA [auth t]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
D, FA [auth f], R, TA [auth t]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
D, FA [auth f], R, TA [auth t]	IPR050115	Proteasome subunit alpha	Family
D, FA [auth f], R, TA [auth t]	IPR023332	Proteasome alpha-type subunit	Family
D, FA [auth f], R, TA [auth t]	IPR001353	Proteasome, subunit alpha/beta	Family
E, GA [auth g], S, UA [auth u]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
E, GA [auth g], S, UA [auth u]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
E, GA [auth g], S, UA [auth u]	IPR050115	Proteasome subunit alpha	Family
E, GA [auth g], S, UA [auth u]	IPR035144	Proteasome subunit alpha 1	Family
E, GA [auth g], S, UA [auth u]	IPR023332	Proteasome alpha-type subunit	Family
E, GA [auth g], S, UA [auth u]	IPR001353	Proteasome, subunit alpha/beta	Family
F, HA [auth h], T, VA [auth v]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
F, HA [auth h], T, VA [auth v]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
F, HA [auth h], T, VA [auth v]	IPR050115	Proteasome subunit alpha	Family
F, HA [auth h], T, VA [auth v]	IPR023332	Proteasome alpha-type subunit	Family
F, HA [auth h], T, VA [auth v]	IPR001353	Proteasome, subunit alpha/beta	Family
G, IA [auth i], U, WA [auth w]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
G, IA [auth i], U, WA [auth w]	IPR034642	Proteasome subunit alpha6	Family
G, IA [auth i], U, WA [auth w]	IPR000426	Proteasome alpha-subunit, N-terminal domain	Domain
G, IA [auth i], U, WA [auth w]	IPR050115	Proteasome subunit alpha	Family
G, IA [auth i], U, WA [auth w]	IPR023332	Proteasome alpha-type subunit	Family
G, IA [auth i], U, WA [auth w]	IPR001353	Proteasome, subunit alpha/beta	Family
H, JA [auth j], V, XA [auth x]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
H, JA [auth j], V, XA [auth x]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
H, JA [auth j], V, XA [auth x]	IPR024689	Proteasome beta subunit, C-terminal	Domain
H, JA [auth j], V, XA [auth x]	IPR023333	Proteasome B-type subunit	Family
H, JA [auth j], V, XA [auth x]	IPR001353	Proteasome, subunit alpha/beta	Family
H, JA [auth j], V, XA [auth x]	IPR000243	Peptidase T1A, proteasome beta-subunit	Family
I, KA [auth k], W, YA [auth y]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
I, KA [auth k], W, YA [auth y]	IPR023333	Proteasome B-type subunit	Family
I, KA [auth k], W, YA [auth y]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
I, KA [auth k], W, YA [auth y]	IPR001353	Proteasome, subunit alpha/beta	Family
I, KA [auth k], W, YA [auth y]	IPR033811	Proteasome beta 3 subunit	Family
AB [auth 1], K, MA [auth m], Y	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
AB [auth 1], K, MA [auth m], Y	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
AB [auth 1], K, MA [auth m], Y	IPR023333	Proteasome B-type subunit	Family
AB [auth 1], K, MA [auth m], Y	IPR001353	Proteasome, subunit alpha/beta	Family
AB [auth 1], K, MA [auth m], Y	IPR000243	Peptidase T1A, proteasome beta-subunit	Family
AA [auth a], CB [auth 3], M, OA [auth o]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
AA [auth a], CB [auth 3], M, OA [auth o]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
AA [auth a], CB [auth 3], M, OA [auth o]	IPR023333	Proteasome B-type subunit	Family
AA [auth a], CB [auth 3], M, OA [auth o]	IPR016295	Proteasome subunit beta 4	Family
AA [auth a], CB [auth 3], M, OA [auth o]	IPR001353	Proteasome, subunit alpha/beta	Family
BA [auth b], DB [auth 4], N, PA [auth p]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
BA [auth b], DB [auth 4], N, PA [auth p]	IPR023333	Proteasome B-type subunit	Family
BA [auth b], DB [auth 4], N, PA [auth p]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
BA [auth b], DB [auth 4], N, PA [auth p]	IPR001353	Proteasome, subunit alpha/beta	Family
BA [auth b], DB [auth 4], N, PA [auth p]	IPR000243	Peptidase T1A, proteasome beta-subunit	Family
J, LA [auth l], X, ZA [auth z]	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
J, LA [auth l], X, ZA [auth z]	IPR023333	Proteasome B-type subunit	Family
J, LA [auth l], X, ZA [auth z]	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
J, LA [auth l], X, ZA [auth z]	IPR050115	Proteasome subunit alpha	Family
J, LA [auth l], X, ZA [auth z]	IPR001353	Proteasome, subunit alpha/beta	Family
J, LA [auth l], X, ZA [auth z]	IPR035206	Proteasome subunit beta 2	Family
BB [auth 2], L, NA [auth n], Z	IPR016050	Proteasome beta-type subunit, conserved site	Conserved Site
BB [auth 2], L, NA [auth n], Z	IPR023333	Proteasome B-type subunit	Family
BB [auth 2], L, NA [auth n], Z	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
BB [auth 2], L, NA [auth n], Z	IPR001353	Proteasome, subunit alpha/beta	Family