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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad5lf3a_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Od5lf3o_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Bd5lf3b_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Pd5lf3p_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Cd5lf3c_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Qd5lf3q_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Dd5lf3d_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Rd5lf3r_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Fd5lf3f_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Td5lf3t_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Gd5lf3g_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ud5lf3u_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Hd5lf3h_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Vd5lf3v_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Id5lf3i_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Wd5lf3w_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Jd5lf3j_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Xd5lf3x_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Kd5lf3k_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Yd5lf3y_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ld5lf3l_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Zd5lf3z_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Md5lf3m_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Nd5lf3n1 Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Nd5lf3n2 Artifacts Tags Tags Tags N-terminal Tags (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ed5lf3e_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Sd5lf3s_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyClass II glutamine amidotransferases 8064014 3000131 SCOP2B (2022-06-29)
OSCOP2B SuperfamilyClass II glutamine amidotransferases 8064014 3000131 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyClass II glutamine amidotransferases 8064036 3000131 SCOP2B (2022-06-29)
PSCOP2B SuperfamilyClass II glutamine amidotransferases 8064036 3000131 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyClass II glutamine amidotransferases 8064004 3000131 SCOP2B (2022-06-29)
QSCOP2B SuperfamilyClass II glutamine amidotransferases 8064004 3000131 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyClass II glutamine amidotransferases 8064022 3000131 SCOP2B (2022-06-29)
RSCOP2B SuperfamilyClass II glutamine amidotransferases 8064022 3000131 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyClass II glutamine amidotransferases 8064054 3000131 SCOP2B (2022-06-29)
TSCOP2B SuperfamilyClass II glutamine amidotransferases 8064054 3000131 SCOP2B (2022-06-29)
HSCOP2B SuperfamilyClass II glutamine amidotransferases 8064074 3000131 SCOP2B (2022-06-29)
VSCOP2B SuperfamilyClass II glutamine amidotransferases 8064074 3000131 SCOP2B (2022-06-29)
KSCOP2B SuperfamilyClass II glutamine amidotransferases 8079492 3000131 SCOP2B (2022-06-29)
YSCOP2B SuperfamilyClass II glutamine amidotransferases 8079492 3000131 SCOP2B (2022-06-29)
BA [auth b]SCOP2B SuperfamilyClass II glutamine amidotransferases 8079175 3000131 SCOP2B (2022-06-29)
NSCOP2B SuperfamilyClass II glutamine amidotransferases 8079175 3000131 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyClass II glutamine amidotransferases 8064060 3000131 SCOP2B (2022-06-29)
SSCOP2B SuperfamilyClass II glutamine amidotransferases 8064060 3000131 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AProteasomee5lf3A1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
OProteasomee5lf3O1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
BProteasomee5lf3B1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
PProteasomee5lf3P1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
CProteasomee5lf3C1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
QProteasomee5lf3Q1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
DProteasomee5lf3D1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
RProteasomee5lf3R1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
FProteasomee5lf3F1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
TProteasomee5lf3T1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
GProteasomee5lf3G1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
UProteasomee5lf3U1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
HProteasomee5lf3H1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
VProteasomee5lf3V1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
IProteasomee5lf3I1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
WProteasomee5lf3W1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
JProteasomee5lf3J1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
XProteasomee5lf3X1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
KProteasomee5lf3K1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
YProteasomee5lf3Y1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
LProteasomee5lf3L1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
ZProteasomee5lf3Z1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
AA [auth a]Proteasomee5lf3a1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
MProteasomee5lf3M1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
BA [auth b]Proteasomee5lf3b1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
NProteasomee5lf3N1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
EProteasomee5lf3E1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
SProteasomee5lf3S1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.60.20.10 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)
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)
D3.60.20.10 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)
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)
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)
K3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
Y3.60.20.10 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)
Z3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (4.3.0)
AA [auth a]3.60.20.10 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)
BA [auth b]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)
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)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
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
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
B, P
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
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
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
F, T
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
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
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
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
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 a],
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 b],
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
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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, O
Proteasome subunit alpha type-2-
B, P
Proteasome subunit alpha type-4-
C, Q
Proteasome subunit alpha type-7
D, R
Proteasome subunit alpha type-5-
F, T
Proteasome subunit alpha type-3
G, U
Proteasome subunit alpha type-6
H, V
Proteasome subunit beta type-7
I, W
Proteasome subunit beta type-3-
J, X
Proteasome subunit beta type-2-
K, Y
Proteasome subunit beta type-5
L, Z
Proteasome subunit beta type-1-
AA [auth a],
M
Proteasome subunit beta type-4
BA [auth b],
N
Proteasome subunit beta type-6
E, S
Proteasome subunit alpha type-1

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A, O
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
A, O
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
A, O
IPR050115Proteasome subunit alphaFamily
A, O
IPR023332Proteasome alpha-type subunitFamily
A, O
IPR001353Proteasome, subunit alpha/betaFamily
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
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
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
D, R
IPR033812Proteasome subunit alpha5Family
D, R
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
D, R
IPR050115Proteasome subunit alphaFamily
D, R
IPR023332Proteasome alpha-type subunitFamily
D, R
IPR001353Proteasome, subunit alpha/betaFamily
F, T
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
F, T
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
F, T
IPR050115Proteasome subunit alphaFamily
F, T
IPR023332Proteasome alpha-type subunitFamily
F, T
IPR001353Proteasome, subunit alpha/betaFamily
G, U
IPR034642Proteasome subunit alpha6Family
G, U
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
G, U
IPR050115Proteasome subunit alphaFamily
G, U
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
G, U
IPR023332Proteasome alpha-type subunitFamily
G, U
IPR001353Proteasome, subunit alpha/betaFamily
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
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
I, W
IPR023333Proteasome B-type subunitFamily
I, W
IPR001353Proteasome, subunit alpha/betaFamily
I, W
IPR033811Proteasome beta 3 subunitFamily
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
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
L, Z
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
L, Z
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
L, Z
IPR023333Proteasome B-type subunitFamily
L, Z
IPR001353Proteasome, subunit alpha/betaFamily
AA [auth a],
M
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
AA [auth a],
M
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
AA [auth a],
M
IPR023333Proteasome B-type subunitFamily
AA [auth a],
M
IPR016295Proteasome subunit beta 4Family
AA [auth a],
M
IPR001353Proteasome, subunit alpha/betaFamily
BA [auth b],
N
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
BA [auth b],
N
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
BA [auth b],
N
IPR023333Proteasome B-type subunitFamily
BA [auth b],
N
IPR001353Proteasome, subunit alpha/betaFamily
BA [auth b],
N
IPR000243Peptidase T1A, proteasome beta-subunitFamily
E, S
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
E, S
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
E, S
IPR050115Proteasome subunit alphaFamily
E, S
IPR035144Proteasome subunit alpha 1Family
E, S
IPR023332Proteasome alpha-type subunitFamily
E, S
IPR001353Proteasome, subunit alpha/betaFamily

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A, O
PharosP25787
B, P
PharosP25789
C, Q
PharosO14818
D, R
PharosP28066
F, T
PharosP25788
G, U
PharosP60900
H, V
PharosQ99436
I, W
PharosP49720
J, X
PharosP49721
K, Y
PharosP28074
L, Z
PharosP20618
AA [auth a],
M
PharosP28070
BA [auth b],
N
PharosP28072
E, S
PharosP25786