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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Pd6reyp_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Cd6reyc_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Qd6reyq_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Dd6reyd_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Rd6reyr_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ed6reye_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Sd6reys_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Td6reyt_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Fd6reyf_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Gd6reyg_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ud6reyu_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Hd6reyh_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Vd6reyv_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Id6reyi_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Wd6reyw_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits automated matches Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Jd6reyj_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Xd6reyx_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
BA [auth b]d6reyb_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Nd6reyn_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ad6reya_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Od6reyo_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome alpha subunit (non-catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Kd6reyk_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Yd6reyy_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Ld6reyl_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Zd6reyz_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Md6reym_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) Proteasome subunits Proteasome beta subunit (catalytic) Human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
BSCOP2B SuperfamilyClass II glutamine amidotransferases8064014 3000131 SCOP2B (2022-06-29)
PSCOP2B SuperfamilyClass II glutamine amidotransferases8064014 3000131 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyClass II glutamine amidotransferases8064036 3000131 SCOP2B (2022-06-29)
QSCOP2B SuperfamilyClass II glutamine amidotransferases8064036 3000131 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyClass II glutamine amidotransferases8064004 3000131 SCOP2B (2022-06-29)
RSCOP2B SuperfamilyClass II glutamine amidotransferases8064004 3000131 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyClass II glutamine amidotransferases8064022 3000131 SCOP2B (2022-06-29)
SSCOP2B SuperfamilyClass II glutamine amidotransferases8064022 3000131 SCOP2B (2022-06-29)
TSCOP2B SuperfamilyClass II glutamine amidotransferases8064060 3000131 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyClass II glutamine amidotransferases8064060 3000131 SCOP2B (2022-06-29)
GSCOP2B SuperfamilyClass II glutamine amidotransferases8064054 3000131 SCOP2B (2022-06-29)
USCOP2B SuperfamilyClass II glutamine amidotransferases8064054 3000131 SCOP2B (2022-06-29)
HSCOP2B SuperfamilyClass II glutamine amidotransferases8079175 3000131 SCOP2B (2022-06-29)
VSCOP2B SuperfamilyClass II glutamine amidotransferases8079175 3000131 SCOP2B (2022-06-29)
ISCOP2B SuperfamilyClass II glutamine amidotransferases8064074 3000131 SCOP2B (2022-06-29)
WSCOP2B SuperfamilyClass II glutamine amidotransferases8064074 3000131 SCOP2B (2022-06-29)
LSCOP2B SuperfamilyClass II glutamine amidotransferases8079492 3000131 SCOP2B (2022-06-29)
ZSCOP2B SuperfamilyClass II glutamine amidotransferases8079492 3000131 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BProteasomee6reyB1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
PProteasomee6reyP1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
CProteasomee6reyC1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
QProteasomee6reyQ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
DProteasomee6reyD1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
RProteasomee6reyR1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
EProteasomee6reyE1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
SProteasomee6reyS1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
TProteasomee6reyT1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
FProteasomee6reyF1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
GProteasomee6reyG1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
UProteasomee6reyU1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
HProteasomee6reyH1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
VProteasomee6reyV1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
IProteasomee6reyI1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
WProteasomee6reyW1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
JProteasomee6reyJ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
XProteasomee6reyX1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
BA [auth b]Proteasomee6reyb1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
NProteasomee6reyN1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
CA [auth c]BLM10_mid,CLASP_N_2e6reyc1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome activator BLM10 (From Topology)T: Proteasome activator BLM10F: BLM10_mid,CLASP_N_2ECOD (1.6)
DA [auth d]BLM10_mid,CLASP_N_2e6reyd1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome activator BLM10 (From Topology)T: Proteasome activator BLM10F: BLM10_mid,CLASP_N_2ECOD (1.6)
AProteasomee6reyA1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
OProteasomee6reyO1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
KProteasomee6reyK1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
YProteasomee6reyY1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
LProteasomee6reyL1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
ZProteasomee6reyZ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
AA [auth a]Proteasomee6reya1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
MProteasomee6reyM1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

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

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
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
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
D, R
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
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
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
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
I, W
PF12465Proteasome beta subunits C terminal (Pr_beta_C)Proteasome beta subunits C terminal- 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
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
CA [auth c],
DA [auth d]
PF16507Proteasome-substrate-size regulator, mid region (BLM10_mid)Proteasome-substrate-size regulator, mid region- Family
CA [auth c],
DA [auth d]
PF11919Domain of unknown function (DUF3437) (DUF3437)Domain of unknown function (DUF3437)- Family
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
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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

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

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
B, P
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
B, P
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
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
IPR023332Proteasome alpha-type subunitFamily
C, Q
IPR001353Proteasome, subunit alpha/betaFamily
D, R
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
D, R
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
D, R
IPR023332Proteasome alpha-type subunitFamily
D, R
IPR001353Proteasome, subunit alpha/betaFamily
E, S
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
E, S
IPR033812Proteasome subunit alpha5Family
E, S
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
E, S
IPR023332Proteasome alpha-type subunitFamily
E, S
IPR001353Proteasome, subunit alpha/betaFamily
F, T
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
F, T
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
F, T
IPR035144Proteasome subunit alpha 1Family
F, T
IPR023332Proteasome alpha-type subunitFamily
F, T
IPR001353Proteasome, subunit alpha/betaFamily
G, U
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
G, U
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
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
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
IPR024689Proteasome beta subunit, C-terminalDomain
I, W
IPR023333Proteasome B-type subunitFamily
I, W
IPR001353Proteasome, subunit alpha/betaFamily
I, W
IPR000243Peptidase T1A, proteasome beta-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
IPR001353Proteasome, subunit alpha/betaFamily
J, X
IPR033811Proteasome beta 3 subunitFamily
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
IPR016295Proteasome subunit beta 4Family
BA [auth b],
N
IPR001353Proteasome, subunit alpha/betaFamily
CA [auth c],
DA [auth d]
IPR032430Proteasome activator Blm10, mid regionDomain
CA [auth c],
DA [auth d]
IPR016024Armadillo-type foldHomologous Superfamily
CA [auth c],
DA [auth d]
IPR021843Proteasome activator complex subunit 4 C-terminal domainDomain
CA [auth c],
DA [auth d]
IPR011989Armadillo-like helicalHomologous Superfamily
CA [auth c],
DA [auth d]
IPR035309Proteasome activator complex subunit 4Family
A, O
IPR034642Proteasome subunit alpha6Family
A, O
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
A, O
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
A, O
IPR023332Proteasome alpha-type subunitFamily
A, O
IPR001353Proteasome, subunit alpha/betaFamily
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
IPR035206Proteasome subunit beta 2Family
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
L, Z
IPR000243Peptidase T1A, proteasome beta-subunitFamily
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
IPR001353Proteasome, subunit alpha/betaFamily

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
B, P
PharosP25787
C, Q
PharosP25789
D, R
PharosO14818
E, S
PharosP28066
F, T
PharosP25786
G, U
PharosP25788
H, V
PharosP28072
I, W
PharosQ99436
J, X
PharosP49720
BA [auth b],
N
PharosP28070
CA [auth c],
DA [auth d]
PharosQ14997
A, O
PharosP60900
K, Y
PharosP49721
L, Z
PharosP28074
AA [auth a],
M
PharosP20618