5VFP

Nucleotide-driven Triple-state Remodeling of the AAA-ATPase Channel in the Activated Human 26S Proteasome


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
B [auth H]SCOP2B SuperfamilyClass II glutamine amidotransferases8064014 3000131 SCOP2B (2022-06-29)
Z [auth h]SCOP2B SuperfamilyClass II glutamine amidotransferases8064014 3000131 SCOP2B (2022-06-29)
DA [auth l]SCOP2B SuperfamilyClass II glutamine amidotransferases8064060 3000131 SCOP2B (2022-06-29)
F [auth L]SCOP2B SuperfamilyClass II glutamine amidotransferases8064060 3000131 SCOP2B (2022-06-29)
EA [auth m]SCOP2B SuperfamilyClass II glutamine amidotransferases8064054 3000131 SCOP2B (2022-06-29)
G [auth M]SCOP2B SuperfamilyClass II glutamine amidotransferases8064054 3000131 SCOP2B (2022-06-29)
FA [auth n]SCOP2B SuperfamilyClass II glutamine amidotransferases8079175 3000131 SCOP2B (2022-06-29)
H [auth N]SCOP2B SuperfamilyClass II glutamine amidotransferases8079175 3000131 SCOP2B (2022-06-29)
GA [auth o]SCOP2B SuperfamilyClass II glutamine amidotransferases8064074 3000131 SCOP2B (2022-06-29)
I [auth O]SCOP2B SuperfamilyClass II glutamine amidotransferases8064074 3000131 SCOP2B (2022-06-29)
JA [auth r]SCOP2B SuperfamilyClass II glutamine amidotransferases8079492 3000131 SCOP2B (2022-06-29)
L [auth R]SCOP2B SuperfamilyClass II glutamine amidotransferases8079492 3000131 SCOP2B (2022-06-29)
MA [auth X]SCOP2B SuperfamilyWinged helix DNA-binding domain8067905 3000034 SCOP2B (2022-06-29)
R [auth Y]SCOP2B SuperfamilyWinged helix DNA-binding domain8057047 3000034 SCOP2B (2022-06-29)
R [auth Y]SCOP2B SuperfamilyTPR-like8057045 3001345 SCOP2B (2022-06-29)
S [auth Z]SCOP2B SuperfamilyJAB1/MPN domain-like8053252 3001105 SCOP2B (2022-06-29)
S [auth Z]SCOP2B SuperfamilyEIF3 subunit F C-terminal domain-like8053251 3002167 SCOP2B (2022-06-29)
V [auth c]SCOP2B SuperfamilyEIF3 subunit F C-terminal domain-like8053254 3002167 SCOP2B (2022-06-29)
V [auth c]SCOP2B SuperfamilyJAB1/MPN domain-like8053255 3001105 SCOP2B (2022-06-29)
AA [auth i]SCOP2B SuperfamilyClass II glutamine amidotransferases8064036 3000131 SCOP2B (2022-06-29)
C [auth I]SCOP2B SuperfamilyClass II glutamine amidotransferases8064036 3000131 SCOP2B (2022-06-29)
BA [auth j]SCOP2B SuperfamilyClass II glutamine amidotransferases8064004 3000131 SCOP2B (2022-06-29)
D [auth J]SCOP2B SuperfamilyClass II glutamine amidotransferases8064004 3000131 SCOP2B (2022-06-29)
CA [auth k]SCOP2B SuperfamilyClass II glutamine amidotransferases8064022 3000131 SCOP2B (2022-06-29)
E [auth K]SCOP2B SuperfamilyClass II glutamine amidotransferases8064022 3000131 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
B [auth H]PF00227,PF10584e5vfpH1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
Z [auth h]PF00227,PF10584e5vfph1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
DA [auth l]PF00227,PF10584e5vfpl1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
F [auth L]PF00227,PF10584e5vfpL1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
EA [auth m]PF00227,PF10584e5vfpm1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
G [auth M]PF00227,PF10584e5vfpM1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
FA [auth n]PF00227e5vfpn1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
H [auth N]PF00227e5vfpN1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
GA [auth o]PF00227,PF12465e5vfpo1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF12465ECOD (1.6)
I [auth O]PF00227,PF12465e5vfpO1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF12465ECOD (1.6)
HA [auth p]PF00227e5vfpp1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
J [auth P]PF00227e5vfpP1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
JA [auth r]PF00227e5vfpr1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
L [auth R]PF00227e5vfpR1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
KA [auth s]PF00227e5vfps1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
M [auth S]PF00227e5vfpS1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
LA [auth t]PF00227e5vfpt1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
N [auth T]PF00227e5vfpT1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
T [auth a]PF01399e5vfpa1 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
T [auth a]PF22037e5vfpa2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF22037ECOD (1.6)
T [auth a]F_UNCLASSIFIEDe5vfpa3 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: F_UNCLASSIFIEDECOD (1.6)
W [auth d]PF10075e5vfpd2 A: alpha arraysX: HTHH: HTHT: wingedF: PF10075ECOD (1.6)
W [auth d]PF10075e5vfpd1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF10075ECOD (1.6)
MA [auth X]PF01399e5vfpX2 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
MA [auth X]PF18055e5vfpX3 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF18055ECOD (1.6)
MA [auth X]PF18503e5vfpX1 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)
OA [auth B]PF16450e5vfpB2 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
OA [auth B]PF17862e5vfpB3 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
OA [auth B]PF00004e5vfpB1 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 G]PF00227,PF10584e5vfpG1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
Y [auth g]PF00227,PF10584e5vfpg1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
IA [auth q]PF00227e5vfpq1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
K [auth Q]PF00227e5vfpQ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
O [auth U]PF18004e5vfpU1 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)
O [auth U]PF21505e5vfpU3 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)
O [auth U]PF01851e5vfpU2 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome/cyclosome (PC) repeat (From Topology)T: Proteasome/cyclosome (PC) repeatF: PF01851ECOD (1.6)
P [auth V]PF01399e5vfpV3 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
P [auth V]F_UNCLASSIFIEDe5vfpV2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: F_UNCLASSIFIEDECOD (1.6)
P [auth V]PF08375e5vfpV1 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)
Q [auth W]PF01399e5vfpW1 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
Q [auth W]PF22241e5vfpW2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF22241ECOD (1.6)
Q [auth W]PF18098e5vfpW3 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)
R [auth Y]PF01399e5vfpY2 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
R [auth Y]PF10602e5vfpY1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF10602ECOD (1.6)
R [auth Y]PF21154e5vfpY3 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)
S [auth Z]PF01398e5vfpZ2 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398ECOD (1.6)
S [auth Z]PF13012e5vfpZ1 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)
U [auth b]PF13519e5vfpb1 A: a/b three-layered sandwichesX: HAD domain-likeH: HAD domain-relatedT: vWA-likeF: PF13519ECOD (1.6)
V [auth c]PF01398e5vfpc1 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398ECOD (1.6)
V [auth c]F_UNCLASSIFIEDe5vfpc2 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)
NA [auth A]PF17862e5vfpA1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
NA [auth A]PF00004e5vfpA3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
QA [auth D]PF16450e5vfpD2 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
QA [auth D]PF17862e5vfpD3 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
QA [auth D]PF00004e5vfpD1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
AA [auth i]PF00227,PF10584e5vfpi1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
C [auth I]PF00227,PF10584e5vfpI1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
RA [auth E]PF16450e5vfpE1 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
RA [auth E]PF17862e5vfpE2 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
RA [auth E]PF00004e5vfpE3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
SA [auth F]PF16450e5vfpF1 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
SA [auth F]PF17862e5vfpF3 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
SA [auth F]PF00004e5vfpF2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
TA [auth f]PF17781e5vfpf2 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)
TA [auth f]PF01851e5vfpf3 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome/cyclosome (PC) repeat (From Topology)T: Proteasome/cyclosome (PC) repeatF: PF01851ECOD (1.6)
BA [auth j]PF00227,PF10584e5vfpj1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
D [auth J]PF00227,PF10584e5vfpJ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
CA [auth k]PF00227,PF10584e5vfpk1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
E [auth K]PF00227,PF10584e5vfpK1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
B [auth H],
Z [auth h]
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 H],
Z [auth h]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
DA [auth l],
F [auth L]
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
DA [auth l],
F [auth L]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
EA [auth m],
G [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
EA [auth m],
G [auth M]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
FA [auth n],
H [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
GA [auth o],
I [auth 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
GA [auth o],
I [auth O]
PF12465Proteasome beta subunits C terminal (Pr_beta_C)Proteasome beta subunits C terminal- Family
HA [auth p],
J [auth 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
JA [auth r],
L [auth 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
KA [auth s],
M [auth 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
LA [auth t],
N [auth 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
T [auth a]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
W [auth d]PF10075CSN8/PSMD8/EIF3K family (CSN8_PSD8_EIF3K)CSN8/PSMD8/EIF3K family- Family
MA [auth X]PF1805526S proteasome regulatory subunit RPN6 N-terminal domain (RPN6_N)26S proteasome regulatory subunit RPN6 N-terminal domain- Repeat
MA [auth X]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
MA [auth X]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
OA [auth B]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
OA [auth B]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
OA [auth B]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
PA [auth C]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
PA [auth C]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
PA [auth C]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 G],
Y [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
A [auth G],
Y [auth g]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
IA [auth q],
K [auth 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
O [auth U]PF13646HEAT repeats (HEAT_2)HEAT repeats- Repeat
O [auth U]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
O [auth U]PF01851Proteasome/cyclosome repeat (PC_rep)Proteasome/cyclosome repeat- Repeat
P [auth V]PF08375Proteasome regulatory subunit C-terminal (Rpn3_C)Proteasome regulatory subunit C-terminal- Family
P [auth V]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
Q [auth W]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
Q [auth W]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
R [auth Y]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
R [auth Y]PF1060226S proteasome subunit RPN7 (RPN7)26S proteasome subunit RPN7- Repeat
R [auth Y]PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
S [auth Z]PF13012Maintenance of mitochondrial structure and function (MitMem_reg)Maintenance of mitochondrial structure and function- Family
S [auth Z]PF01398JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)JAB1/Mov34/MPN/PAD-1 ubiquitin protease- Family
U [auth b]PF13519von Willebrand factor type A domain (VWA_2)von Willebrand factor type A domain- Domain
V [auth c]PF01398JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)JAB1/Mov34/MPN/PAD-1 ubiquitin protease- Family
NA [auth A]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
NA [auth A]PF2123626S proteasome regulatory subunit 7, OB domain (PRS7_OB)26S proteasome regulatory subunit 7, OB domainThis is the OB domain from 26S proteasome regulatory subunit 7 (PRS7, also known as PSMC2, Rpt1 or MSS1), a component of the 19S proteasome cap [1-5]. These are one of six ATPases of the regulatory particle that form a heterohexameric ring. This doma ...This is the OB domain from 26S proteasome regulatory subunit 7 (PRS7, also known as PSMC2, Rpt1 or MSS1), a component of the 19S proteasome cap [1-5]. These are one of six ATPases of the regulatory particle that form a heterohexameric ring. This domain mediates interactions with USP14 or Ubp6 [2,4].
Domain
NA [auth A]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
QA [auth D]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
QA [auth D]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
QA [auth D]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
AA [auth i],
C [auth I]
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 i],
C [auth I]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
RA [auth E]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
RA [auth E]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
RA [auth E]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
SA [auth F]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
SA [auth F]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
SA [auth F]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
TA [auth f]PF01851Proteasome/cyclosome repeat (PC_rep)Proteasome/cyclosome repeat- Repeat
BA [auth j],
D [auth J]
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 j],
D [auth J]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
CA [auth k],
E [auth K]
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 k],
E [auth K]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
B [auth H],
Z [auth h]
Proteasome subunit alpha type-2-
DA [auth l],
F [auth L]
Proteasome subunit alpha type-1
EA [auth m],
G [auth M]
Proteasome subunit alpha type-3
FA [auth n],
H [auth N]
Proteasome subunit beta type-6
GA [auth o],
I [auth O]
Proteasome subunit beta type-7
HA [auth p],
J [auth P]
Proteasome subunit beta type-3-
JA [auth r],
L [auth R]
Proteasome subunit beta type-5
KA [auth s],
M [auth S]
Proteasome subunit beta type-1-
LA [auth t],
N [auth T]
Proteasome subunit beta type-4
T [auth a]26S proteasome non-ATPase regulatory subunit 13
W [auth d]26S proteasome non-ATPase regulatory subunit 8-
X [auth e]sem1---
MA [auth X]26S proteasome non-ATPase regulatory subunit 11
OA [auth B]26S proteasome regulatory subunit 4
PA [auth C]26S proteasome regulatory subunit 8
A [auth G],
Y [auth g]
Proteasome subunit alpha type-6
IA [auth q],
K [auth Q]
Proteasome subunit beta type-2-
O [auth U]26S proteasome non-ATPase regulatory subunit 1
P [auth V]26S proteasome non-ATPase regulatory subunit 3
Q [auth W]26S proteasome non-ATPase regulatory subunit 12-
R [auth Y]26S proteasome non-ATPase regulatory subunit 6-
S [auth Z]26S proteasome non-ATPase regulatory subunit 7
U [auth b]26S proteasome non-ATPase regulatory subunit 4
V [auth c]26S proteasome non-ATPase regulatory subunit 14
NA [auth A]26S proteasome regulatory subunit 7
QA [auth D]26S proteasome regulatory subunit 6B
AA [auth i],
C [auth I]
Proteasome subunit alpha type-4-
RA [auth E]26S proteasome regulatory subunit 10B
SA [auth F]26S proteasome regulatory subunit 6A
TA [auth f]26S proteasome non-ATPase regulatory subunit 2
BA [auth j],
D [auth J]
Proteasome subunit alpha type-7
CA [auth k],
E [auth K]
Proteasome subunit alpha type-5-

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
B [auth H],
Z [auth h]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
B [auth H],
Z [auth h]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
B [auth H],
Z [auth h]
IPR023332Proteasome alpha-type subunitFamily
B [auth H],
Z [auth h]
IPR001353Proteasome, subunit alpha/betaFamily
DA [auth l],
F [auth L]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
DA [auth l],
F [auth L]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
DA [auth l],
F [auth L]
IPR035144Proteasome subunit alpha 1Family
DA [auth l],
F [auth L]
IPR023332Proteasome alpha-type subunitFamily
DA [auth l],
F [auth L]
IPR001353Proteasome, subunit alpha/betaFamily
EA [auth m],
G [auth M]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
EA [auth m],
G [auth M]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
EA [auth m],
G [auth M]
IPR023332Proteasome alpha-type subunitFamily
EA [auth m],
G [auth M]
IPR001353Proteasome, subunit alpha/betaFamily
FA [auth n],
H [auth N]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
FA [auth n],
H [auth N]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
FA [auth n],
H [auth N]
IPR023333Proteasome B-type subunitFamily
FA [auth n],
H [auth N]
IPR001353Proteasome, subunit alpha/betaFamily
FA [auth n],
H [auth N]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
GA [auth o],
I [auth O]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
GA [auth o],
I [auth O]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
GA [auth o],
I [auth O]
IPR024689Proteasome beta subunit, C-terminalDomain
GA [auth o],
I [auth O]
IPR023333Proteasome B-type subunitFamily
GA [auth o],
I [auth O]
IPR001353Proteasome, subunit alpha/betaFamily
GA [auth o],
I [auth O]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
HA [auth p],
J [auth P]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
HA [auth p],
J [auth P]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
HA [auth p],
J [auth P]
IPR023333Proteasome B-type subunitFamily
HA [auth p],
J [auth P]
IPR001353Proteasome, subunit alpha/betaFamily
HA [auth p],
J [auth P]
IPR033811Proteasome beta 3 subunitFamily
JA [auth r],
L [auth R]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
JA [auth r],
L [auth R]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
JA [auth r],
L [auth R]
IPR023333Proteasome B-type subunitFamily
JA [auth r],
L [auth R]
IPR001353Proteasome, subunit alpha/betaFamily
JA [auth r],
L [auth R]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
KA [auth s],
M [auth S]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
KA [auth s],
M [auth S]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
KA [auth s],
M [auth S]
IPR023333Proteasome B-type subunitFamily
KA [auth s],
M [auth S]
IPR001353Proteasome, subunit alpha/betaFamily
LA [auth t],
N [auth T]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
LA [auth t],
N [auth T]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
LA [auth t],
N [auth T]
IPR023333Proteasome B-type subunitFamily
LA [auth t],
N [auth T]
IPR016295Proteasome subunit beta 4Family
LA [auth t],
N [auth T]
IPR001353Proteasome, subunit alpha/betaFamily
T [auth a]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
T [auth a]IPR03529826S Proteasome non-ATPase regulatory subunit 13Family
T [auth a]IPR000717Proteasome component (PCI) domainDomain
W [auth d]IPR000717Proteasome component (PCI) domainDomain
W [auth d]IPR00674626S proteasome non-ATPase regulatory subunit Rpn12Family
W [auth d]IPR033464CSN8/PSMD8/EIF3KDomain
MA [auth X]IPR0407806S proteasome subunit Rpn6, C-terminal helix domainDomain
MA [auth X]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
MA [auth X]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
MA [auth X]IPR04077326S proteasome regulatory subunit Rpn6, N-terminalDomain
MA [auth X]IPR000717Proteasome component (PCI) domainDomain
OA [auth B]IPR041569AAA ATPase, AAA+ lid domainDomain
OA [auth B]IPR032501Proteasomal ATPase, second OB domainDomain
OA [auth B]IPR003960ATPase, AAA-type, conserved siteConserved Site
OA [auth B]IPR003593AAA+ ATPase domainDomain
OA [auth B]IPR003959ATPase, AAA-type, coreDomain
OA [auth B]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
OA [auth B]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
PA [auth C]IPR003593AAA+ ATPase domainDomain
PA [auth C]IPR003959ATPase, AAA-type, coreDomain
PA [auth C]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
PA [auth C]IPR041569AAA ATPase, AAA+ lid domainDomain
PA [auth C]IPR032501Proteasomal ATPase, second OB domainDomain
PA [auth C]IPR003960ATPase, AAA-type, conserved siteConserved Site
PA [auth C]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
A [auth G],
Y [auth g]
IPR034642Proteasome subunit alpha6Family
A [auth G],
Y [auth g]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
A [auth G],
Y [auth g]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
A [auth G],
Y [auth g]
IPR023332Proteasome alpha-type subunitFamily
A [auth G],
Y [auth g]
IPR001353Proteasome, subunit alpha/betaFamily
IA [auth q],
K [auth Q]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
IA [auth q],
K [auth Q]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
IA [auth q],
K [auth Q]
IPR023333Proteasome B-type subunitFamily
IA [auth q],
K [auth Q]
IPR001353Proteasome, subunit alpha/betaFamily
IA [auth q],
K [auth Q]
IPR035206Proteasome subunit beta 2Family
O [auth U]IPR04062326S proteasome regulatory subunit RPN2, C-terminalDomain
O [auth U]IPR016024Armadillo-type foldHomologous Superfamily
O [auth U]IPR002015Proteasome/cyclosome repeatRepeat
O [auth U]IPR011989Armadillo-like helicalHomologous Superfamily
O [auth U]IPR04857026S proteasome non-ATPase regulatory subunit 1/RPN2, N-terminal domainDomain
O [auth U]IPR01664226S proteasome regulatory complex, non-ATPase subcomplex, Rpn2/Psmd1 subunitFamily
P [auth V]IPR01358626S proteasome regulatory subunit, C-terminalDomain
P [auth V]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
P [auth V]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
P [auth V]IPR000717Proteasome component (PCI) domainDomain
Q [auth W]IPR036388Winged helix-like DNA-binding domain superfamilyHomologous Superfamily
Q [auth W]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
Q [auth W]IPR000717Proteasome component (PCI) domainDomain
Q [auth W]IPR04089626S proteasome regulatory subunit RPN5, C-terminal domainDomain
Q [auth W]IPR04013426S Proteasome non-ATPase regulatory subunit 12/COP9 signalosome complex subunit 4Family
R [auth Y]IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
R [auth Y]IPR01958526S proteasome regulatory subunit Rpn7/COP9 signalosome complex subunit 1Family
R [auth Y]IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
R [auth Y]IPR04954926S proteasome regulatory subunit RPN7/PSMD6, C-terminal helixDomain
R [auth Y]IPR000717Proteasome component (PCI) domainDomain
R [auth Y]IPR04513526S proteasome regulatory subunit Rpn7, N-terminalDomain
S [auth Z]IPR03385826S Proteasome non-ATPase regulatory subunit 7/8Family
S [auth Z]IPR024969EIF3F/CSN6-like, C-terminalDomain
S [auth Z]IPR037518MPN domainDomain
S [auth Z]IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain
U [auth b]IPR036465von Willebrand factor A-like domain superfamilyHomologous Superfamily
U [auth b]IPR002035von Willebrand factor, type ADomain
U [auth b]IPR003903Ubiquitin interacting motifConserved Site
U [auth b]IPR049590PSMD4, RAZUL domainDomain
V [auth c]IPR037518MPN domainDomain
V [auth c]IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain
NA [auth A]IPR003593AAA+ ATPase domainDomain
NA [auth A]IPR003959ATPase, AAA-type, coreDomain
NA [auth A]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
NA [auth A]IPR04872326S proteasome regulatory subunit 7-like, OB domainDomain
NA [auth A]IPR041569AAA ATPase, AAA+ lid domainDomain
NA [auth A]IPR003960ATPase, AAA-type, conserved siteConserved Site
NA [auth A]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
QA [auth D]IPR041569AAA ATPase, AAA+ lid domainDomain
QA [auth D]IPR032501Proteasomal ATPase, second OB domainDomain
QA [auth D]IPR003960ATPase, AAA-type, conserved siteConserved Site
QA [auth D]IPR003593AAA+ ATPase domainDomain
QA [auth D]IPR003959ATPase, AAA-type, coreDomain
QA [auth D]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
QA [auth D]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
AA [auth i],
C [auth I]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
AA [auth i],
C [auth I]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
AA [auth i],
C [auth I]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
AA [auth i],
C [auth I]
IPR023332Proteasome alpha-type subunitFamily
AA [auth i],
C [auth I]
IPR001353Proteasome, subunit alpha/betaFamily
RA [auth E]IPR003593AAA+ ATPase domainDomain
RA [auth E]IPR003959ATPase, AAA-type, coreDomain
RA [auth E]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
RA [auth E]IPR041569AAA ATPase, AAA+ lid domainDomain
RA [auth E]IPR032501Proteasomal ATPase, second OB domainDomain
RA [auth E]IPR003960ATPase, AAA-type, conserved siteConserved Site
RA [auth E]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
SA [auth F]IPR003593AAA+ ATPase domainDomain
SA [auth F]IPR003959ATPase, AAA-type, coreDomain
SA [auth F]IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
SA [auth F]IPR041569AAA ATPase, AAA+ lid domainDomain
SA [auth F]IPR032501Proteasomal ATPase, second OB domainDomain
SA [auth F]IPR003960ATPase, AAA-type, conserved siteConserved Site
SA [auth F]IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
TA [auth f]IPR04143326S proteasome non-ATPase regulatory subunit RPN1, C-terminalDomain
TA [auth f]IPR016024Armadillo-type foldHomologous Superfamily
TA [auth f]IPR002015Proteasome/cyclosome repeatRepeat
TA [auth f]IPR01664326S proteasome regulatory complex, non-ATPase subcomplex, Rpn1 subunitFamily
TA [auth f]IPR011989Armadillo-like helicalHomologous Superfamily
TA [auth f]IPR040892RPN1, N-terminalDomain
BA [auth j],
D [auth J]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
BA [auth j],
D [auth J]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
BA [auth j],
D [auth J]
IPR023332Proteasome alpha-type subunitFamily
BA [auth j],
D [auth J]
IPR001353Proteasome, subunit alpha/betaFamily
CA [auth k],
E [auth K]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
CA [auth k],
E [auth K]
IPR033812Proteasome subunit alpha5Family
CA [auth k],
E [auth K]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
CA [auth k],
E [auth K]
IPR023332Proteasome alpha-type subunitFamily
CA [auth k],
E [auth K]
IPR001353Proteasome, subunit alpha/betaFamily

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
B [auth H],
Z [auth h]
PharosP25787
DA [auth l],
F [auth L]
PharosP25786
EA [auth m],
G [auth M]
PharosP25788
FA [auth n],
H [auth N]
PharosP28072
GA [auth o],
I [auth O]
PharosQ99436
HA [auth p],
J [auth P]
PharosP49720
JA [auth r],
L [auth R]
PharosP28074
KA [auth s],
M [auth S]
PharosP20618
LA [auth t],
N [auth T]
PharosP28070
T [auth a]PharosQ9UNM6
W [auth d]PharosP48556
MA [auth X]PharosO00231
PA [auth C]PharosP62195
A [auth G],
Y [auth g]
PharosP60900
IA [auth q],
K [auth Q]
PharosP49721
O [auth U]PharosQ99460
P [auth V]PharosO43242
Q [auth W]PharosO00232
R [auth Y]PharosQ15008
S [auth Z]PharosP51665
U [auth b]PharosP55036
V [auth c]PharosO00487
NA [auth A]PharosP35998
QA [auth D]PharosP43686
AA [auth i],
C [auth I]
PharosP25789
SA [auth F]PharosP17980
TA [auth f]PharosQ13200
BA [auth j],
D [auth J]
PharosO14818
CA [auth k],
E [auth K]
PharosP28066