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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad6qm7a_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Od6qm7o_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Xd6qm7x_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Jd6qm7j_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Kd6qm7k_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Yd6qm7y_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Zd6qm7z_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Ld6qm7l_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Md6qm7m_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
BA [auth b]d6qm7b_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Nd6qm7n_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Pd6qm7p_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Dd6qm7d_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Rd6qm7r_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Ed6qm7e_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Sd6qm7s_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Fd6qm7f_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Td6qm7t_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Gd6qm7g_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Ud6qm7u_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Wd6qm7w_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)
Id6qm7i_ Alpha and beta proteins (a+b) Ntn hydrolase-like N-terminal nucleophile aminohydrolases (Ntn hydrolases) automated matches automated matches (Leishmania tarentolae ) [TaxId: 5689 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyClass II glutamine amidotransferases8095639 3000131 SCOP2B (2022-06-29)
OSCOP2B SuperfamilyClass II glutamine amidotransferases8095639 3000131 SCOP2B (2022-06-29)
ZSCOP2B SuperfamilyClass II glutamine amidotransferases8097106 3000131 SCOP2B (2022-06-29)
LSCOP2B SuperfamilyClass II glutamine amidotransferases8097106 3000131 SCOP2B (2022-06-29)
AA [auth a]SCOP2 FamilyProteasome subunits8097091 4002254 SCOP2 (2022-06-29)
AA [auth a]SCOP2 SuperfamilyClass II glutamine amidotransferases8097092 3000131 SCOP2 (2022-06-29)
MSCOP2B SuperfamilyClass II glutamine amidotransferases8097092 3000131 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyClass II glutamine amidotransferases8095699 3000131 SCOP2B (2022-06-29)
PSCOP2B SuperfamilyClass II glutamine amidotransferases8095699 3000131 SCOP2B (2022-06-29)
CSCOP2 FamilyProteasome subunits8097095 4002254 SCOP2 (2022-06-29)
CSCOP2 SuperfamilyClass II glutamine amidotransferases8097096 3000131 SCOP2 (2022-06-29)
QSCOP2B SuperfamilyClass II glutamine amidotransferases8097096 3000131 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyClass II glutamine amidotransferases8095675 3000131 SCOP2B (2022-06-29)
RSCOP2 FamilyProteasome subunits8095674 4002254 SCOP2 (2022-06-29)
RSCOP2 SuperfamilyClass II glutamine amidotransferases8095675 3000131 SCOP2 (2022-06-29)
ESCOP2B SuperfamilyClass II glutamine amidotransferases8095589 3000131 SCOP2B (2022-06-29)
SSCOP2B SuperfamilyClass II glutamine amidotransferases8095589 3000131 SCOP2B (2022-06-29)
FSCOP2 FamilyProteasome subunits8097103 4002254 SCOP2 (2022-06-29)
FSCOP2 SuperfamilyClass II glutamine amidotransferases8097104 3000131 SCOP2 (2022-06-29)
TSCOP2B SuperfamilyClass II glutamine amidotransferases8097104 3000131 SCOP2B (2022-06-29)
GSCOP2 FamilyProteasome subunits8097099 4002254 SCOP2 (2022-06-29)
GSCOP2 SuperfamilyClass II glutamine amidotransferases8097100 3000131 SCOP2 (2022-06-29)
USCOP2B SuperfamilyClass II glutamine amidotransferases8097100 3000131 SCOP2B (2022-06-29)
VSCOP2B SuperfamilyClass II glutamine amidotransferases8097094 3000131 SCOP2B (2022-06-29)
HSCOP2B SuperfamilyClass II glutamine amidotransferases8097094 3000131 SCOP2B (2022-06-29)
WSCOP2 FamilyProteasome subunits8097089 4002254 SCOP2 (2022-06-29)
WSCOP2 SuperfamilyClass II glutamine amidotransferases8097090 3000131 SCOP2 (2022-06-29)
ISCOP2B SuperfamilyClass II glutamine amidotransferases8097090 3000131 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF00227,PF10584e6qm7A1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
OPF00227,PF10584e6qm7O1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
XPF00227e6qm7X1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
JPF00227e6qm7J1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
KPF00227e6qm7K1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
YPF00227e6qm7Y1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
ZPF00227e6qm7Z1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
LPF00227e6qm7L1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
AA [auth a]PF00227e6qm7a1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
MPF00227e6qm7M1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
BA [auth b]PF00227e6qm7b1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
NPF00227e6qm7N1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
BPF00227,PF10584e6qm7B1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
PPF00227,PF10584e6qm7P1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
CPF00227,PF10584e6qm7C1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
QPF00227,PF10584e6qm7Q1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
DPF00227,PF10584e6qm7D1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
RPF00227,PF10584e6qm7R1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
EPF00227,PF10584e6qm7E1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
SPF00227,PF10584e6qm7S1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
FPF00227,PF10584e6qm7F1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
TPF00227,PF10584e6qm7T1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
GPF00227,PF10584e6qm7G1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
UPF00227,PF10584e6qm7U1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
WPF00227e6qm7W1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
IPF00227e6qm7I1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (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 (utative)
O3.60.20.10 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)
J3.60.20.10 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)
Z3.60.20.10 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)
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)
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)
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)
F3.60.20.10 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)
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)
V3.60.20.10 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)
W3.60.20.10 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)

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
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
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
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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, O
Proteasome alpha1 chain-
J, X
Proteasome beta3 chain
K, Y
Proteasome beta4 chain
L, Z
Proteasome beta5 chain
AA [auth a],
M
Proteasome beta6 chain-
BA [auth b],
N
Proteasome beta7 chain-
B, P
Proteasome alpha2 chain
C, Q
Proteasome alpha3 chain
D, R
Proteasome alpha4 chain
E, S
Proteasome alpha5 chain
F, T
Proteasome alpha6 chain
G, U
Proteasome alpha7 chain
H, V
Proteasome beta1 chain
I, W
Proteasome beta2 chain

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
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
A, O
IPR034642Proteasome subunit alpha6Family
J, X
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
J, X
IPR023333Proteasome B-type subunitFamily
J, X
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
J, X
IPR001353Proteasome, subunit alpha/betaFamily
J, X
IPR033811Proteasome beta 3 subunitFamily
K, Y
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
K, Y
IPR001353Proteasome, subunit alpha/betaFamily
K, Y
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
L, Z
IPR000243Peptidase T1A, proteasome beta-subunitFamily
AA [auth a],
M
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
AA [auth a],
M
IPR023333Proteasome B-type subunitFamily
AA [auth a],
M
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
AA [auth a],
M
IPR001353Proteasome, subunit alpha/betaFamily
BA [auth b],
N
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
BA [auth b],
N
IPR023333Proteasome B-type subunitFamily
BA [auth b],
N
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
BA [auth b],
N
IPR016295Proteasome subunit beta 4Family
BA [auth b],
N
IPR001353Proteasome, subunit alpha/betaFamily
B, P
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
B, P
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
B, P
IPR023332Proteasome alpha-type subunitFamily
B, P
IPR001353Proteasome, subunit alpha/betaFamily
C, Q
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
C, Q
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
C, Q
IPR023332Proteasome alpha-type subunitFamily
C, Q
IPR001353Proteasome, subunit alpha/betaFamily
D, R
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
D, R
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
D, R
IPR023332Proteasome alpha-type subunitFamily
D, R
IPR001353Proteasome, subunit alpha/betaFamily
E, S
IPR033812Proteasome subunit alpha5Family
E, S
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
E, S
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
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
IPR035144Proteasome subunit alpha 1Family
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
IPR023332Proteasome alpha-type subunitFamily
G, U
IPR001353Proteasome, subunit alpha/betaFamily
H, V
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
H, V
IPR023333Proteasome B-type subunitFamily
H, V
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
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
IPR000243Peptidase T1A, proteasome beta-subunitFamily