5MPB

26S proteasome in presence of AMP-PNP (s3)


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
A [auth a]SCOP2B SuperfamilyClass II glutamine amidotransferases8036842 3000131 SCOP2B (2022-06-29)
O [auth A]SCOP2B SuperfamilyClass II glutamine amidotransferases8036842 3000131 SCOP2B (2022-06-29)
L [auth l]SCOP2B SuperfamilyClass II glutamine amidotransferases8079504 3000131 SCOP2B (2022-06-29)
Z [auth 5]SCOP2B SuperfamilyClass II glutamine amidotransferases8079504 3000131 SCOP2B (2022-06-29)
B [auth b]SCOP2B SuperfamilyClass II glutamine amidotransferases8064048 3000131 SCOP2B (2022-06-29)
P [auth B]SCOP2B SuperfamilyClass II glutamine amidotransferases8064048 3000131 SCOP2B (2022-06-29)
JA [auth V]SCOP2B SuperfamilyJAB1/MPN domain-like8053248 3001105 SCOP2B (2022-06-29)
LA [auth X]SCOP2B SuperfamilyPH domain-like8093403 3000134 SCOP2B (2022-06-29)
C [auth c]SCOP2B SuperfamilyClass II glutamine amidotransferases8064020 3000131 SCOP2B (2022-06-29)
Q [auth C]SCOP2B SuperfamilyClass II glutamine amidotransferases8064020 3000131 SCOP2B (2022-06-29)
SA [auth R]SCOP2B SuperfamilyTPR-like8057042 3001345 SCOP2B (2022-06-29)
SA [auth R]SCOP2B SuperfamilyWinged helix DNA-binding domain8057044 3000034 SCOP2B (2022-06-29)
TA [auth U]SCOP2B SuperfamilyEIF3 subunit F C-terminal domain-like8053273 3002167 SCOP2B (2022-06-29)
TA [auth U]SCOP2B SuperfamilyJAB1/MPN domain-like8053272 3001105 SCOP2B (2022-06-29)
D [auth d]SCOP2B SuperfamilyClass II glutamine amidotransferases8064012 3000131 SCOP2B (2022-06-29)
R [auth D]SCOP2B SuperfamilyClass II glutamine amidotransferases8064012 3000131 SCOP2B (2022-06-29)
E [auth e]SCOP2B SuperfamilyClass II glutamine amidotransferases8064026 3000131 SCOP2B (2022-06-29)
S [auth E]SCOP2B SuperfamilyClass II glutamine amidotransferases8064026 3000131 SCOP2B (2022-06-29)
F [auth f]SCOP2B SuperfamilyClass II glutamine amidotransferases8064066 3000131 SCOP2B (2022-06-29)
T [auth F]SCOP2B SuperfamilyClass II glutamine amidotransferases8064066 3000131 SCOP2B (2022-06-29)
G [auth g]SCOP2B SuperfamilyClass II glutamine amidotransferases8079169 3000131 SCOP2B (2022-06-29)
U [auth G]SCOP2B SuperfamilyClass II glutamine amidotransferases8079169 3000131 SCOP2B (2022-06-29)
H [auth h]SCOP2B SuperfamilyClass II glutamine amidotransferases8036787 3000131 SCOP2B (2022-06-29)
V [auth 1]SCOP2B SuperfamilyClass II glutamine amidotransferases8036787 3000131 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
CA [auth H]PF17862e5mpbH2 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
DA [auth I]PF16450e5mpbI1 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
DA [auth I]PF17862e5mpbI2 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
DA [auth I]PF00004e5mpbI3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
A [auth a]PF00227,PF10584e5mpba1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
O [auth A]PF00227,PF10584e5mpbA1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
J [auth j]PF00227e5mpbj1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
X [auth 3]PF00227e5mpb31 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
K [auth k]PF00227e5mpbk1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
Y [auth 4]PF00227e5mpb41 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
L [auth l]PF00227e5mpbl1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
Z [auth 5]PF00227e5mpb51 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
AA [auth 6]PF00227e5mpb61 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
M [auth m]PF00227e5mpbm1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
BA [auth 7]PF00227e5mpb71 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
N [auth n]PF00227e5mpbn1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
FA [auth L]PF16450e5mpbL1 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
FA [auth L]PF17862e5mpbL2 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
FA [auth L]PF00004e5mpbL3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
GA [auth M]PF16450e5mpbM2 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
GA [auth M]PF17862e5mpbM1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
GA [auth M]PF00004e5mpbM3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
B [auth b]PF00227,PF10584e5mpbb1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
P [auth B]PF00227,PF10584e5mpbB1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
IA [auth W]PF13519e5mpbW1 A: a/b three-layered sandwichesX: HAD domain-likeH: HAD domain-relatedT: vWA-likeF: PF13519ECOD (1.6)
JA [auth V]PF01398e5mpbV1 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398ECOD (1.6)
JA [auth V]F_UNCLASSIFIEDe5mpbV2 A: extended segmentsX: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domainF: F_UNCLASSIFIEDECOD (1.6)
KA [auth T]PF10075e5mpbT1 A: alpha arraysX: HTHH: HTHT: wingedF: PF10075ECOD (1.6)
KA [auth T]PF10075e5mpbT2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF10075ECOD (1.6)
LA [auth X]PF04683e5mpbX1 A: beta barrelsX: PH domain-likeH: PH domain-like (From Topology)T: PH domain-likeF: PF04683ECOD (1.6)
NA [auth Z]PF17781e5mpbZ2 A: alpha superhelicesX: Repetitive alpha hairpinsH: 26S proteasome subunit Rpn2 N-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 N-terminal domainF: PF17781ECOD (1.6)
NA [auth Z]PF01851,PF18051e5mpbZ1 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome/cyclosome (PC) repeat (From Topology)T: Proteasome/cyclosome (PC) repeatF: PF01851,PF18051ECOD (1.6)
OA [auth N]PF18004e5mpbN1 A: beta sandwichesX: 26S proteasome subunit Rpn2 C-terminal domain (From Topology)H: 26S proteasome subunit Rpn2 C-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 C-terminal domainF: PF18004ECOD (1.6)
OA [auth N]PF21505e5mpbN2 A: alpha superhelicesX: Repetitive alpha hairpinsH: 26S proteasome subunit Rpn2 N-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 N-terminal domainF: PF21505ECOD (1.6)
OA [auth N]PF01851e5mpbN3 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome/cyclosome (PC) repeat (From Topology)T: Proteasome/cyclosome (PC) repeatF: PF01851ECOD (1.6)
PA [auth S]PF01399e5mpbS1 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
PA [auth S]F_UNCLASSIFIEDe5mpbS2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: F_UNCLASSIFIEDECOD (1.6)
PA [auth S]PF08375e5mpbS3 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN3 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN3 C-terminal helixF: PF08375ECOD (1.6)
QA [auth P]PF01399e5mpbP1 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
QA [auth P]PF22241e5mpbP2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF22241ECOD (1.6)
QA [auth P]PF18098e5mpbP3 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN5 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN5 C-terminal helixF: PF18098ECOD (1.6)
C [auth c]PF00227,PF10584e5mpbc1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
Q [auth C]PF00227,PF10584e5mpbC1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
RA [auth Q]PF01399e5mpbQ3 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
RA [auth Q]PF18055e5mpbQ2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF18055ECOD (1.6)
RA [auth Q]PF18503e5mpbQ1 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN6 C-termial helix (From Topology)T: 26S proteasome regulatory subunit RPN6 C-termial helixF: PF18503ECOD (1.6)
SA [auth R]PF01399e5mpbR3 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
SA [auth R]PF10602e5mpbR2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF10602ECOD (1.6)
SA [auth R]PF21154e5mpbR1 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN7 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN7 C-terminal helixF: PF21154ECOD (1.6)
TA [auth U]PF01398e5mpbU1 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398ECOD (1.6)
TA [auth U]PF13012e5mpbU2 A: extended segmentsX: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domainF: PF13012ECOD (1.6)
UA [auth O]PF01399e5mpbO1 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
UA [auth O]PF22037e5mpbO3 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF22037ECOD (1.6)
UA [auth O]PF18261e5mpbO2 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN9 C-terminal helixF: PF18261ECOD (1.6)
D [auth d]PF00227,PF10584e5mpbd1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
R [auth D]PF00227,PF10584e5mpbD1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
E [auth e]PF00227,PF10584e5mpbe1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
S [auth E]PF00227,PF10584e5mpbE1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
F [auth f]PF00227,PF10584e5mpbf1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
T [auth F]PF00227,PF10584e5mpbF1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
G [auth g]PF00227,PF10584e5mpbg1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
U [auth G]PF00227,PF10584e5mpbG1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
H [auth h]PF00227e5mpbh1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
V [auth 1]PF00227e5mpb11 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
I [auth i]PF00227,PF12465e5mpbi1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF12465ECOD (1.6)
W [auth 2]PF00227,PF12465e5mpb21 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF12465ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
CA [auth H]PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
CA [auth H]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
DA [auth I]PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2]Domain
DA [auth I]PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
DA [auth I]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
A [auth a],
O [auth A]
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 [auth a],
O [auth A]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
J [auth j],
X [auth 3]
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 [auth k],
Y [auth 4]
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 [auth l],
Z [auth 5]
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 6],
M [auth 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 7],
N [auth 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
EA [auth K]PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2]Domain
EA [auth K]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
FA [auth L]PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2]Domain
FA [auth L]PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
FA [auth L]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
GA [auth M]PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2]Domain
GA [auth M]PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
GA [auth M]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
B [auth b],
P [auth B]
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 [auth b],
P [auth B]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
HA [auth J]PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2]Domain
HA [auth J]PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
HA [auth J]PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
IA [auth W]PF13519von Willebrand factor type A domain (VWA_2)von Willebrand factor type A domain- Domain
JA [auth V]PF01398JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)JAB1/Mov34/MPN/PAD-1 ubiquitin protease- Family
KA [auth T]PF10075CSN8/PSMD8/EIF3K family (CSN8_PSD8_EIF3K)CSN8/PSMD8/EIF3K family- Family
LA [auth X]PF04683Proteasome complex subunit Rpn13, Pru domain (Rpn13_ADRM1_Pru)Proteasome complex subunit Rpn13, Pru domainThis family was thought originally to be involved in cell-adhesion [1,2], but the members are now known to be proteasome subunit Rpn13, a novel ubiquitin receptor. The 26S proteasome is a huge macromolecular protein-degradation machine consisting of ...This family was thought originally to be involved in cell-adhesion [1,2], but the members are now known to be proteasome subunit Rpn13, a novel ubiquitin receptor. The 26S proteasome is a huge macromolecular protein-degradation machine consisting of a proteolytically active 20S core, in the form of four disc-like proteins, and one or two 19S regulatory particles. The regulatory particle(s) sit on the top and or bottom of the core, de-ubiquitinate the substrate peptides, unfold them and guide them into the narrow channel through the centre of the core. Rpn13 and its homologues dock onto the regulatory particle through the N-terminal region which binds Rpn2. The C-terminal part of the domain binds de-ubiquitinating enzyme Uch37/UCHL5 and enhances its isopeptidase activity. Rpn13 binds ubiquitin via a conserved amino-terminal region called the pleckstrin-like receptor for ubiquitin, termed Pru, domain [4]. The domain forms two contiguous anti-parallel beta-sheets with a configuration similar to the pleckstrin-homology domain (PHD) fold [5]. Rpn13's ability to bind ubiquitin and the proteasome subunit Rpn2/S1 simultaneously supports evidence of its role as a ubiquitin receptor. Finally, when complexed to di-ubiquitin, via the Pru, and Uch37 via the C-terminal part, it frees up the distal ubiquitin for de-ubiquitination by the Uch37 [5].
Domain
MA [auth Y]PF05160DSS1/SEM1 family (DSS1_SEM1)DSS1/SEM1 family- Family
NA [auth Z]PF17781RPN1 N-terminal domain (RPN1_RPN2_N)RPN1 N-terminal domainThis domain is found at the N-terminus of the 26S proteasome regulatory subunits RPN1 (also known as 26S proteasome non-ATPase regulatory subunit 2 (PMSD2)[1]. The domain is formed by an array of alpha helices [2].Domain
NA [auth Z]PF01851Proteasome/cyclosome repeat (PC_rep)Proteasome/cyclosome repeat- Repeat
NA [auth Z]PF1805126S proteasome non-ATPase regulatory subunit RPN1 C-terminal (RPN1_C)26S proteasome non-ATPase regulatory subunit RPN1 C-terminalThis is the C-terminal domain found in RPN1 proteins (26S proteasome non-ATPase regulatory subunit 2). The 26S proteasome holocomplex consists of a 28-subunit barrel-shaped core particle (CP) in the center capped at the top and bottom by 19-subunit ...This is the C-terminal domain found in RPN1 proteins (26S proteasome non-ATPase regulatory subunit 2). The 26S proteasome holocomplex consists of a 28-subunit barrel-shaped core particle (CP) in the center capped at the top and bottom by 19-subunit regulatory particles (RPs). The CP forms the catalytic chamber and the RP is formed from two subcomplexes known as the lid and the base [1]. The lid comprises nine Rpn subunits in yeast (Rpn3/5/6/7/8/9/11/12/15) and the base comprises three Rpn subunits (Rpn1/2/13) and six ATPases (Rpt1-6) [2].
Domain
OA [auth N]PF13646HEAT repeats (HEAT_2)HEAT repeats- Repeat
OA [auth N]PF1800426S proteasome regulatory subunit RPN2 C-terminal domain (RPN2_C)26S proteasome regulatory subunit RPN2 C-terminal domainThis is the C-terminal domain found in S. cerevisiae Rpn2 (26S proteasome regulatory subunit RPN2) as well as other eukaryotic species. A study revealed that the C-terminal 52 residues of the Rpn2 C-terminal domain are responsible for mediating inter ...This is the C-terminal domain found in S. cerevisiae Rpn2 (26S proteasome regulatory subunit RPN2) as well as other eukaryotic species. A study revealed that the C-terminal 52 residues of the Rpn2 C-terminal domain are responsible for mediating interactions with the ubiquitin-binding subunit Rpn13. Futhermore, the extreme C-terminal 20 or 21 residues of Rpn2 (926-945 or 925-945) of S. cerevisiae, were shown to be equally effective at binding Rpn13. Multiple sequence alignments indicate that Rpn2 orthologs are highly conserved in this C-terminal region and share characteristic acidic, aromatic, and proline residues, suggesting a common function. In the structure of Rpn2 from S. cerevisiae , this region is exposed and disordered, and is thus accessible for associating with Rpn13. The Rpn2 binding surface of human Rpn13 has been mapped by nuclear magnetic resonance titration to one surface of its Pru domain [1].
Domain
OA [auth N]PF2150526S proteasome subunit RPN2, N-terminal domain (RPN2_N)26S proteasome subunit RPN2, N-terminal domainThis entry represents the N-terminal helical domain of 26S proteasome regulatory subunit RPN2 and 26S proteasome non-ATPase regulatory subunit 1 (PSMD1). It adopts a rod-like structure [1-5].Domain
OA [auth N]PF01851Proteasome/cyclosome repeat (PC_rep)Proteasome/cyclosome repeat- Repeat
PA [auth S]PF08375Proteasome regulatory subunit C-terminal (Rpn3_C)Proteasome regulatory subunit C-terminal- Family
PA [auth S]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
QA [auth P]PF1809826S proteasome regulatory subunit RPN5 C-terminal domain (RPN5_C)26S proteasome regulatory subunit RPN5 C-terminal domainThis is the C-terminal domain of the 26S proteasome regulatory subunit RPN5 proteins.This helical domain can be found adjacent to Pfam:PF01399. The 26S proteasome is the major ATP-dependent protease in eukaryotes. Three subcomplexes form this degrada ...This is the C-terminal domain of the 26S proteasome regulatory subunit RPN5 proteins.This helical domain can be found adjacent to Pfam:PF01399. The 26S proteasome is the major ATP-dependent protease in eukaryotes. Three subcomplexes form this degradation machine: the lid, the base, and the core. The helices found at the C terminus of each lid subunit form a helical bundle that directs the ordered self-assembly of the lid subcomplex. This domain which comprises the tail of RPN5 along with the tail of Rpn9, are important for Rpn12 binding to the lid [1].
Domain
QA [auth P]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
C [auth c],
Q [auth C]
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 [auth c],
Q [auth C]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
RA [auth Q]PF1805526S proteasome regulatory subunit RPN6 N-terminal domain (RPN6_N)26S proteasome regulatory subunit RPN6 N-terminal domain- Repeat
RA [auth Q]PF1850326S proteasome subunit RPN6 C-terminal helix domain (RPN6_C_helix)26S proteasome subunit RPN6 C-terminal helix domainThis is the C-terminal helix domain found in RPN6, a component of the 26S proteasome. The C-terminal helices are essential for lid assembly [1, 2].Domain
RA [auth Q]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
SA [auth R]PF2115426S proteasome regulatory subunit RPN7/PSMD6 C-terminal helix (RPN7_PSMD6_C)26S proteasome regulatory subunit RPN7/PSMD6 C-terminal helixRPN7/PSDM6 are regulatory subunits from the 26S proteasome. This entry represents the C-terminal helix.Domain
SA [auth R]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
SA [auth R]PF1060226S proteasome subunit RPN7 (RPN7)26S proteasome subunit RPN7- Repeat
TA [auth U]PF13012Maintenance of mitochondrial structure and function (MitMem_reg)Maintenance of mitochondrial structure and function- Family
TA [auth U]PF01398JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)JAB1/Mov34/MPN/PAD-1 ubiquitin protease- Family
UA [auth O]PF18261Rpn9 C-terminal helix (Rpn9_C)Rpn9 C-terminal helix- Family
UA [auth O]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
D [auth d],
R [auth D]
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 [auth d],
R [auth D]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
E [auth e],
S [auth E]
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 [auth e],
S [auth E]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
F [auth f],
T [auth F]
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 [auth f],
T [auth F]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
G [auth g],
U [auth G]
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 [auth g],
U [auth G]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
H [auth h],
V [auth 1]
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 [auth i],
W [auth 2]
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 [auth i],
W [auth 2]
PF12465Proteasome beta subunits C terminal (Pr_beta_C)Proteasome beta subunits C terminal- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
CA [auth H]26S protease regulatory subunit 7 homolog
DA [auth I]26S protease regulatory subunit 4 homolog
A [auth a],
O [auth A]
Proteasome subunit alpha type-1-
J [auth j],
X [auth 3]
Proteasome subunit beta type-3
K [auth k],
Y [auth 4]
Proteasome subunit beta type-4
L [auth l],
Z [auth 5]
Proteasome subunit beta type-5
AA [auth 6],
M [auth m]
Proteasome subunit beta type-6-
BA [auth 7],
N [auth n]
Proteasome subunit beta type-7-
EA [auth K]26S protease regulatory subunit 6B homolog
FA [auth L]26S protease subunit RPT4
GA [auth M]26S protease regulatory subunit 6A
B [auth b],
P [auth B]
Proteasome subunit alpha type-2-
HA [auth J]26S protease regulatory subunit 8 homolog
IA [auth W]26S proteasome regulatory subunit RPN10
JA [auth V]Ubiquitin carboxyl-terminal hydrolase RPN11
KA [auth T]26S proteasome regulatory subunit RPN12-
LA [auth X]26S proteasome regulatory subunit RPN13
MA [auth Y]26S proteasome complex subunit SEM1
NA [auth Z]26S proteasome regulatory subunit RPN1
OA [auth N]26S proteasome regulatory subunit RPN2
PA [auth S]26S proteasome regulatory subunit RPN3
QA [auth P]26S proteasome regulatory subunit RPN5-
C [auth c],
Q [auth C]
Proteasome subunit alpha type-3-
RA [auth Q]26S proteasome regulatory subunit RPN6
SA [auth R]26S proteasome regulatory subunit RPN7
TA [auth U]26S proteasome regulatory subunit RPN8
UA [auth O]26S proteasome regulatory subunit RPN9
D [auth d],
R [auth D]
Proteasome subunit alpha type-4-
E [auth e],
S [auth E]
Proteasome subunit alpha type-5-
F [auth f],
T [auth F]
Proteasome subunit alpha type-6-
G [auth g],
U [auth G]
Probable proteasome subunit alpha type-7
H [auth h],
V [auth 1]
Proteasome subunit beta type-1
I [auth i],
W [auth 2]
Proteasome subunit beta type-2

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
CA [auth H]IPR04872326S proteasome regulatory subunit 7-like, OB domainDomain
CA [auth H]IPR041569AAA ATPase, AAA+ lid domainDomain
CA [auth H]IPR003960ATPase, AAA-type, conserved siteConserved Site
CA [auth H]IPR003593AAA+ ATPase domainDomain
CA [auth H]IPR003959ATPase, AAA-type, coreDomain
CA [auth H]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
CA [auth H]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
DA [auth I]IPR041569AAA ATPase, AAA+ lid domainDomain
DA [auth I]IPR032501Proteasomal ATPase, second OB domainDomain
DA [auth I]IPR003960ATPase, AAA-type, conserved siteConserved Site
DA [auth I]IPR003593AAA+ ATPase domainDomain
DA [auth I]IPR003959ATPase, AAA-type, coreDomain
DA [auth I]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
DA [auth I]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
A [auth a],
O [auth A]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
A [auth a],
O [auth A]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
A [auth a],
O [auth A]
IPR023332Proteasome alpha-type subunitFamily
A [auth a],
O [auth A]
IPR001353Proteasome, subunit alpha/betaFamily
A [auth a],
O [auth A]
IPR034642Proteasome subunit alpha6Family
J [auth j],
X [auth 3]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
J [auth j],
X [auth 3]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
J [auth j],
X [auth 3]
IPR023333Proteasome B-type subunitFamily
J [auth j],
X [auth 3]
IPR001353Proteasome, subunit alpha/betaFamily
J [auth j],
X [auth 3]
IPR033811Proteasome beta 3 subunitFamily
K [auth k],
Y [auth 4]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
K [auth k],
Y [auth 4]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
K [auth k],
Y [auth 4]
IPR023333Proteasome B-type subunitFamily
K [auth k],
Y [auth 4]
IPR001353Proteasome, subunit alpha/betaFamily
K [auth k],
Y [auth 4]
IPR035206Proteasome subunit beta 2Family
L [auth l],
Z [auth 5]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
L [auth l],
Z [auth 5]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
L [auth l],
Z [auth 5]
IPR023333Proteasome B-type subunitFamily
L [auth l],
Z [auth 5]
IPR001353Proteasome, subunit alpha/betaFamily
L [auth l],
Z [auth 5]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
AA [auth 6],
M [auth m]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
AA [auth 6],
M [auth m]
IPR023333Proteasome B-type subunitFamily
AA [auth 6],
M [auth m]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
AA [auth 6],
M [auth m]
IPR001353Proteasome, subunit alpha/betaFamily
BA [auth 7],
N [auth n]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
BA [auth 7],
N [auth n]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
BA [auth 7],
N [auth n]
IPR023333Proteasome B-type subunitFamily
BA [auth 7],
N [auth n]
IPR016295Proteasome subunit beta 4Family
BA [auth 7],
N [auth n]
IPR001353Proteasome, subunit alpha/betaFamily
EA [auth K]IPR032501Proteasomal ATPase, second OB domainDomain
EA [auth K]IPR003960ATPase, AAA-type, conserved siteConserved Site
EA [auth K]IPR003593AAA+ ATPase domainDomain
EA [auth K]IPR003959ATPase, AAA-type, coreDomain
EA [auth K]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
EA [auth K]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
FA [auth L]IPR041569AAA ATPase, AAA+ lid domainDomain
FA [auth L]IPR032501Proteasomal ATPase, second OB domainDomain
FA [auth L]IPR003960ATPase, AAA-type, conserved siteConserved Site
FA [auth L]IPR003593AAA+ ATPase domainDomain
FA [auth L]IPR003959ATPase, AAA-type, coreDomain
FA [auth L]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
FA [auth L]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
GA [auth M]IPR041569AAA ATPase, AAA+ lid domainDomain
GA [auth M]IPR032501Proteasomal ATPase, second OB domainDomain
GA [auth M]IPR003960ATPase, AAA-type, conserved siteConserved Site
GA [auth M]IPR003593AAA+ ATPase domainDomain
GA [auth M]IPR003959ATPase, AAA-type, coreDomain
GA [auth M]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
GA [auth M]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
B [auth b],
P [auth B]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
B [auth b],
P [auth B]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
B [auth b],
P [auth B]
IPR023332Proteasome alpha-type subunitFamily
B [auth b],
P [auth B]
IPR001353Proteasome, subunit alpha/betaFamily
HA [auth J]IPR041569AAA ATPase, AAA+ lid domainDomain
HA [auth J]IPR032501Proteasomal ATPase, second OB domainDomain
HA [auth J]IPR003960ATPase, AAA-type, conserved siteConserved Site
HA [auth J]IPR003593AAA+ ATPase domainDomain
HA [auth J]IPR003959ATPase, AAA-type, coreDomain
HA [auth J]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
HA [auth J]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
IA [auth W]IPR002035von Willebrand factor, type ADomain
IA [auth W]IPR003903Ubiquitin interacting motifConserved Site
IA [auth W]IPR036465von Willebrand factor A-like domain superfamilyHomologous Superfamily
JA [auth V]IPR037518MPN domainDomain
JA [auth V]IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain
KA [auth T]IPR000717Proteasome component (PCI) domainDomain
KA [auth T]IPR00674626S proteasome non-ATPase regulatory subunit Rpn12Family
KA [auth T]IPR033464CSN8/PSMD8/EIF3KDomain
LA [auth X]IPR044868Rpn13/ADRM1, Pru domainDomain
LA [auth X]IPR006773Proteasomal ubiquitin receptor Rpn13/ADRM1Family
LA [auth X]IPR038633Proteasomal ubiquitin receptor Rpn13/ADRM1, Pru domain superfamilyHomologous Superfamily
MA [auth Y]IPR007834DSS1/SEM1Family
NA [auth Z]IPR04143326S proteasome non-ATPase regulatory subunit RPN1, C-terminalDomain
NA [auth Z]IPR016024Armadillo-type foldHomologous Superfamily
NA [auth Z]IPR002015Proteasome/cyclosome repeatRepeat
NA [auth Z]IPR01664326S proteasome regulatory complex, non-ATPase subcomplex, Rpn1 subunitFamily
NA [auth Z]IPR011989Armadillo-like helicalHomologous Superfamily
NA [auth Z]IPR040892RPN1, N-terminalDomain
OA [auth N]IPR04062326S proteasome regulatory subunit RPN2, C-terminalDomain
OA [auth N]IPR016024Armadillo-type foldHomologous Superfamily
OA [auth N]IPR002015Proteasome/cyclosome repeatRepeat
OA [auth N]IPR011989Armadillo-like helicalHomologous Superfamily
OA [auth N]IPR04857026S proteasome non-ATPase regulatory subunit 1/RPN2, N-terminal domainDomain
OA [auth N]IPR01664226S proteasome regulatory complex, non-ATPase subcomplex, Rpn2/Psmd1 subunitFamily
PA [auth S]IPR000717Proteasome component (PCI) domainDomain
PA [auth S]IPR01358626S proteasome regulatory subunit, C-terminalDomain
PA [auth S]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
QA [auth P]IPR000717Proteasome component (PCI) domainDomain
QA [auth P]IPR04089626S proteasome regulatory subunit RPN5, C-terminal domainDomain
QA [auth P]IPR04013426S Proteasome non-ATPase regulatory subunit 12/COP9 signalosome complex subunit 4Family
QA [auth P]IPR036388Winged helix-like DNA-binding domain superfamilyHomologous Superfamily
QA [auth P]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
C [auth c],
Q [auth C]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
C [auth c],
Q [auth C]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
C [auth c],
Q [auth C]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
C [auth c],
Q [auth C]
IPR023332Proteasome alpha-type subunitFamily
C [auth c],
Q [auth C]
IPR001353Proteasome, subunit alpha/betaFamily
RA [auth Q]IPR04077326S proteasome regulatory subunit Rpn6, N-terminalDomain
RA [auth Q]IPR000717Proteasome component (PCI) domainDomain
RA [auth Q]IPR0407806S proteasome subunit Rpn6, C-terminal helix domainDomain
RA [auth Q]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
RA [auth Q]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
SA [auth R]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
SA [auth R]IPR01958526S proteasome regulatory subunit Rpn7/COP9 signalosome complex subunit 1Family
SA [auth R]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
SA [auth R]IPR04954926S proteasome regulatory subunit RPN7/PSMD6, C-terminal helixDomain
SA [auth R]IPR000717Proteasome component (PCI) domainDomain
SA [auth R]IPR04513526S proteasome regulatory subunit Rpn7, N-terminalDomain
SA [auth R]IPR019734Tetratricopeptide repeatRepeat
TA [auth U]IPR024969EIF3F/CSN6-like, C-terminalDomain
TA [auth U]IPR037518MPN domainDomain
TA [auth U]IPR03385826S Proteasome non-ATPase regulatory subunit 7/8Family
TA [auth U]IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain
UA [auth O]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
UA [auth O]IPR03529826S Proteasome non-ATPase regulatory subunit 13Family
UA [auth O]IPR000717Proteasome component (PCI) domainDomain
UA [auth O]IPR040798Rpn9, C-terminal helixDomain
D [auth d],
R [auth D]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
D [auth d],
R [auth D]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
D [auth d],
R [auth D]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
D [auth d],
R [auth D]
IPR023332Proteasome alpha-type subunitFamily
D [auth d],
R [auth D]
IPR001353Proteasome, subunit alpha/betaFamily
E [auth e],
S [auth E]
IPR033812Proteasome subunit alpha5Family
E [auth e],
S [auth E]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
E [auth e],
S [auth E]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
E [auth e],
S [auth E]
IPR023332Proteasome alpha-type subunitFamily
E [auth e],
S [auth E]
IPR001353Proteasome, subunit alpha/betaFamily
F [auth f],
T [auth F]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
F [auth f],
T [auth F]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
F [auth f],
T [auth F]
IPR023332Proteasome alpha-type subunitFamily
F [auth f],
T [auth F]
IPR001353Proteasome, subunit alpha/betaFamily
G [auth g],
U [auth G]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
G [auth g],
U [auth G]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
G [auth g],
U [auth G]
IPR023332Proteasome alpha-type subunitFamily
G [auth g],
U [auth G]
IPR001353Proteasome, subunit alpha/betaFamily
H [auth h],
V [auth 1]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
H [auth h],
V [auth 1]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
H [auth h],
V [auth 1]
IPR023333Proteasome B-type subunitFamily
H [auth h],
V [auth 1]
IPR001353Proteasome, subunit alpha/betaFamily
H [auth h],
V [auth 1]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
I [auth i],
W [auth 2]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
I [auth i],
W [auth 2]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
I [auth i],
W [auth 2]
IPR024689Proteasome beta subunit, C-terminalDomain
I [auth i],
W [auth 2]
IPR023333Proteasome B-type subunitFamily
I [auth i],
W [auth 2]
IPR001353Proteasome, subunit alpha/betaFamily
I [auth i],
W [auth 2]
IPR000243Peptidase T1A, proteasome beta-subunitFamily