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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Yd3mg7y_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Kd3mg7k_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Od3mg7o_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Ad3mg7a_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Jd3mg7j_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Xd3mg7x_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Zd3mg7z_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Ld3mg7l_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Md3mg7m_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
AA [auth 1]d3mg71_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
BA [auth 2]d3mg72_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Nd3mg7n_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Bd3mg7b_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Pd3mg7p_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Cd3mg7c_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Qd3mg7q_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Rd3mg7r_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Dd3mg7d_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Ed3mg7e_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Sd3mg7s_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Fd3mg7f_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Td3mg7t_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Gd3mg7g_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Ud3mg7u_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Hd3mg7h_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Vd3mg7v_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Id3mg7i_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)
Wd3mg7w_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
YSCOP2B SuperfamilyClass II glutamine amidotransferases 8079504 3000131 SCOP2B (2022-06-29)
KSCOP2B SuperfamilyClass II glutamine amidotransferases 8079504 3000131 SCOP2B (2022-06-29)
OSCOP2B SuperfamilyClass II glutamine amidotransferases 8064048 3000131 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyClass II glutamine amidotransferases 8064048 3000131 SCOP2B (2022-06-29)
BA [auth 2]SCOP2B SuperfamilyClass II glutamine amidotransferases 8036787 3000131 SCOP2B (2022-06-29)
NSCOP2B SuperfamilyClass II glutamine amidotransferases 8036787 3000131 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyClass II glutamine amidotransferases 8064020 3000131 SCOP2B (2022-06-29)
PSCOP2B SuperfamilyClass II glutamine amidotransferases 8064020 3000131 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyClass II glutamine amidotransferases 8064012 3000131 SCOP2B (2022-06-29)
QSCOP2B SuperfamilyClass II glutamine amidotransferases 8064012 3000131 SCOP2B (2022-06-29)
RSCOP2B SuperfamilyClass II glutamine amidotransferases 8064026 3000131 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyClass II glutamine amidotransferases 8064026 3000131 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyClass II glutamine amidotransferases 8064066 3000131 SCOP2B (2022-06-29)
SSCOP2B SuperfamilyClass II glutamine amidotransferases 8064066 3000131 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyClass II glutamine amidotransferases 8079169 3000131 SCOP2B (2022-06-29)
TSCOP2B SuperfamilyClass II glutamine amidotransferases 8079169 3000131 SCOP2B (2022-06-29)
GSCOP2B SuperfamilyClass II glutamine amidotransferases 8036842 3000131 SCOP2B (2022-06-29)
USCOP2B SuperfamilyClass II glutamine amidotransferases 8036842 3000131 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
YProteasomee3mg7Y1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
KProteasomee3mg7K1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
OProteasomee3mg7O1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
AProteasomee3mg7A1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
JProteasomee3mg7J1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
XProteasomee3mg7X1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
ZProteasomee3mg7Z1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
LProteasomee3mg7L1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
MProteasomee3mg7M1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
AA [auth 1]Proteasomee3mg711 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
BProteasomee3mg7B1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
PProteasomee3mg7P1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
CProteasomee3mg7C1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
QProteasomee3mg7Q1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
RProteasomee3mg7R1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
DProteasomee3mg7D1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
EProteasomee3mg7E1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
SProteasomee3mg7S1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
FProteasomee3mg7F1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
TProteasomee3mg7T1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
GProteasomee3mg7G1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
UProteasomee3mg7U1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
HProteasomee3mg7H1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
VProteasomee3mg7V1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
IProteasomee3mg7I1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
WProteasomee3mg7W1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
Y3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
K3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
O3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
A3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
J3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
X3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
Z3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
L3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
M3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
AA [auth 1]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
BA [auth 2]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
N3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
B3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
P3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
C3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
Q3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
R3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
D3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
E3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
S3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
F3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
T3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
G3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
U3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
H3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
V3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
I3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
W3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
K, Y
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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, O
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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, O
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
J, X
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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
L, Z
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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 1],
M
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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 2],
N
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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, P
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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, Q
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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, Q
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
D, R
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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, S
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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, S
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
F, T
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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, U
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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, U
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
H, V
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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, V
PF12465Proteasome beta subunits C terminal (Pr_beta_C)Proteasome beta subunits C terminal- Family
I, W
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe 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

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
K, Y
Proteasome component PRE2
A, O
Proteasome component Y7-
J, X
Proteasome component C11
L, Z
Proteasome component C5-
AA [auth 1],
M
Proteasome component PRE4-
BA [auth 2],
N
Proteasome component PRE3
B, P
Proteasome component Y13-
C, Q
Proteasome component PRE6-
D, R
Proteasome component PUP2-
E, S
Proteasome component PRE5-
F, T
Proteasome component C1
G, U
Proteasome component C7-alpha-
H, V
Proteasome component PUP1
I, W
Proteasome component PUP3

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
K, Y
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
K, Y
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
K, Y
IPR023333Proteasome B-type subunitFamily
K, Y
IPR001353Proteasome, subunit alpha/betaFamily
K, Y
IPR000243Peptidase T1A, proteasome beta-subunitFamily
A, O
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
A, O
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
A, O
IPR050115Proteasome subunit alphaFamily
A, O
IPR023332Proteasome alpha-type subunitFamily
A, O
IPR001353Proteasome, subunit alpha/betaFamily
J, X
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
J, X
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
J, X
IPR023333Proteasome B-type subunitFamily
J, X
IPR050115Proteasome subunit alphaFamily
J, X
IPR001353Proteasome, subunit alpha/betaFamily
J, X
IPR035206Proteasome subunit beta 2Family
L, Z
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
L, Z
IPR023333Proteasome B-type subunitFamily
L, Z
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
L, Z
IPR001353Proteasome, subunit alpha/betaFamily
AA [auth 1],
M
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
AA [auth 1],
M
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
AA [auth 1],
M
IPR023333Proteasome B-type subunitFamily
AA [auth 1],
M
IPR016295Proteasome subunit beta 4Family
AA [auth 1],
M
IPR001353Proteasome, subunit alpha/betaFamily
BA [auth 2],
N
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
BA [auth 2],
N
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
BA [auth 2],
N
IPR023333Proteasome B-type subunitFamily
BA [auth 2],
N
IPR001353Proteasome, subunit alpha/betaFamily
BA [auth 2],
N
IPR000243Peptidase T1A, proteasome beta-subunitFamily
B, P
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
B, P
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
B, P
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
B, P
IPR050115Proteasome subunit alphaFamily
B, P
IPR023332Proteasome alpha-type subunitFamily
B, P
IPR001353Proteasome, subunit alpha/betaFamily
C, Q
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
C, Q
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
C, Q
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
C, Q
IPR050115Proteasome subunit alphaFamily
C, Q
IPR023332Proteasome alpha-type subunitFamily
C, Q
IPR001353Proteasome, subunit alpha/betaFamily
D, R
IPR033812Proteasome subunit alpha5Family
D, R
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
D, R
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
D, R
IPR050115Proteasome subunit alphaFamily
D, R
IPR023332Proteasome alpha-type subunitFamily
D, R
IPR001353Proteasome, subunit alpha/betaFamily
E, S
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
E, S
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
E, S
IPR050115Proteasome subunit alphaFamily
E, S
IPR023332Proteasome alpha-type subunitFamily
E, S
IPR001353Proteasome, subunit alpha/betaFamily
F, T
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
F, T
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
F, T
IPR050115Proteasome subunit alphaFamily
F, T
IPR023332Proteasome alpha-type subunitFamily
F, T
IPR001353Proteasome, subunit alpha/betaFamily
G, U
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
G, U
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
G, U
IPR050115Proteasome subunit alphaFamily
G, U
IPR023332Proteasome alpha-type subunitFamily
G, U
IPR001353Proteasome, subunit alpha/betaFamily
G, U
IPR034642Proteasome subunit alpha6Family
H, V
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
H, V
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
H, V
IPR024689Proteasome beta subunit, C-terminalDomain
H, V
IPR023333Proteasome B-type subunitFamily
H, V
IPR001353Proteasome, subunit alpha/betaFamily
H, V
IPR000243Peptidase T1A, proteasome beta-subunitFamily
I, W
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
I, W
IPR023333Proteasome B-type subunitFamily
I, W
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
I, W
IPR001353Proteasome, subunit alpha/betaFamily
I, W
IPR033811Proteasome beta 3 subunitFamily