5MPA
26S proteasome in presence of ATP (s2)
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A [auth a] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8036842 | 3000131 | SCOP2B (2022-06-29) |
O [auth A] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8036842 | 3000131 | SCOP2B (2022-06-29) |
B [auth b] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064048 | 3000131 | SCOP2B (2022-06-29) |
P [auth B] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064048 | 3000131 | SCOP2B (2022-06-29) |
C [auth c] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064020 | 3000131 | SCOP2B (2022-06-29) |
Q [auth C] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064020 | 3000131 | SCOP2B (2022-06-29) |
D [auth d] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064012 | 3000131 | SCOP2B (2022-06-29) |
R [auth D] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064012 | 3000131 | SCOP2B (2022-06-29) |
E [auth e] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064026 | 3000131 | SCOP2B (2022-06-29) |
S [auth E] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064026 | 3000131 | SCOP2B (2022-06-29) |
F [auth f] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064066 | 3000131 | SCOP2B (2022-06-29) |
T [auth F] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8064066 | 3000131 | SCOP2B (2022-06-29) |
G [auth g] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8079169 | 3000131 | SCOP2B (2022-06-29) |
U [auth G] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8079169 | 3000131 | SCOP2B (2022-06-29) |
H [auth h] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8036787 | 3000131 | SCOP2B (2022-06-29) |
V [auth 1] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8036787 | 3000131 | SCOP2B (2022-06-29) |
L [auth l] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8079504 | 3000131 | SCOP2B (2022-06-29) |
Z [auth 5] | SCOP2B Superfamily | Class II glutamine amidotransferases | 8079504 | 3000131 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A [auth a] | PF00227,PF10584 | e5mpaa1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
O [auth A] | PF00227,PF10584 | e5mpaA1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
B [auth b] | PF00227,PF10584 | e5mpab1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
P [auth B] | PF00227,PF10584 | e5mpaB1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
C [auth c] | PF00227,PF10584 | e5mpac1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
Q [auth C] | PF00227,PF10584 | e5mpaC1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
D [auth d] | PF00227,PF10584 | e5mpad1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
R [auth D] | PF00227,PF10584 | e5mpaD1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
E [auth e] | PF00227,PF10584 | e5mpae1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
S [auth E] | PF00227,PF10584 | e5mpaE1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
F [auth f] | PF00227,PF10584 | e5mpaf1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
T [auth F] | PF00227,PF10584 | e5mpaF1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
G [auth g] | PF00227,PF10584 | e5mpag1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
U [auth G] | PF00227,PF10584 | e5mpaG1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
H [auth h] | PF00227 | e5mpah1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
V [auth 1] | PF00227 | e5mpa11 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
I [auth i] | PF00227,PF12465 | e5mpai1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF12465 | ECOD (1.6) |
W [auth 2] | PF00227,PF12465 | e5mpa21 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF12465 | ECOD (1.6) |
X [auth 3] | PF00227 | e5mpa31 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
J [auth j] | PF00227 | e5mpaj1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
K [auth k] | PF00227 | e5mpak1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
Y [auth 4] | PF00227 | e5mpa41 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
L [auth l] | PF00227 | e5mpal1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
Z [auth 5] | PF00227 | e5mpa51 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
AA [auth 6] | PF00227 | e5mpa61 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
M [auth m] | PF00227 | e5mpam1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
BA [auth 7] | PF00227 | e5mpa71 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
N [auth n] | PF00227 | e5mpan1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
CA [auth H] | PF17862 | e5mpaH3 | A: alpha arrays | X: Histone-like | H: Histone-related | T: AAA+ ATPase lid domain | F: PF17862 | ECOD (1.6) |
DA [auth I] | PF16450 | e5mpaI1 | A: beta barrels | X: OB-fold | H: Nucleic acid-binding proteins (From Topology) | T: Nucleic acid-binding proteins | F: PF16450 | ECOD (1.6) |
DA [auth I] | PF17862 | e5mpaI3 | A: alpha arrays | X: Histone-like | H: Histone-related | T: AAA+ ATPase lid domain | F: PF17862 | ECOD (1.6) |
DA [auth I] | PF00004 | e5mpaI2 | A: a/b three-layered sandwiches | X: P-loop domains-like | H: P-loop domains-related | T: P-loop containing nucleoside triphosphate hydrolases | F: PF00004 | ECOD (1.6) |
FA [auth L] | PF16450 | e5mpaL2 | A: beta barrels | X: OB-fold | H: Nucleic acid-binding proteins (From Topology) | T: Nucleic acid-binding proteins | F: PF16450 | ECOD (1.6) |
FA [auth L] | PF17862 | e5mpaL1 | A: alpha arrays | X: Histone-like | H: Histone-related | T: AAA+ ATPase lid domain | F: PF17862 | ECOD (1.6) |
FA [auth L] | PF00004 | e5mpaL3 | A: a/b three-layered sandwiches | X: P-loop domains-like | H: P-loop domains-related | T: P-loop containing nucleoside triphosphate hydrolases | F: PF00004 | ECOD (1.6) |
GA [auth M] | PF16450 | e5mpaM3 | A: beta barrels | X: OB-fold | H: Nucleic acid-binding proteins (From Topology) | T: Nucleic acid-binding proteins | F: PF16450 | ECOD (1.6) |
GA [auth M] | PF17862 | e5mpaM1 | A: alpha arrays | X: Histone-like | H: Histone-related | T: AAA+ ATPase lid domain | F: PF17862 | ECOD (1.6) |
GA [auth M] | PF00004 | e5mpaM2 | A: a/b three-layered sandwiches | X: P-loop domains-like | H: P-loop domains-related | T: P-loop containing nucleoside triphosphate hydrolases | F: PF00004 | ECOD (1.6) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
A [auth a], O [auth A] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
A [auth a], O [auth A] | PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family |
B [auth b], P [auth B] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
B [auth b], P [auth B] | PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family |
C [auth c], Q [auth C] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
C [auth c], Q [auth C] | PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family |
D [auth d], R [auth D] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
D [auth d], R [auth D] | PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family |
E [auth e], S [auth E] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
E [auth e], S [auth E] | PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family |
F [auth f], T [auth F] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
F [auth f], T [auth F] | PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family |
G [auth g], U [auth G] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
G [auth g], U [auth G] | PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family |
H [auth h], V [auth 1] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
I [auth i], W [auth 2] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
I [auth i], W [auth 2] | PF12465 | Proteasome beta subunits C terminal (Pr_beta_C) | Proteasome beta subunits C terminal | - | Family |
J [auth j], X [auth 3] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
K [auth k], Y [auth 4] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
L [auth l], Z [auth 5] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
AA [auth 6], M [auth m] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
BA [auth 7], N [auth n] | PF00227 | Proteasome subunit (Proteasome) | Proteasome subunit | 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 ... | Domain |
CA [auth H] | PF17862 | AAA+ lid domain (AAA_lid_3) | AAA+ lid domain | This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. | Domain |
CA [auth H] | PF00004 | ATPase 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] | PF16450 | Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C) | Proteasomal ATPase OB C-terminal domain | This is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2] | Domain |
DA [auth I] | PF17862 | AAA+ lid domain (AAA_lid_3) | AAA+ lid domain | This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. | Domain |
DA [auth I] | PF00004 | ATPase 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 |
EA [auth K] | PF16450 | Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C) | Proteasomal ATPase OB C-terminal domain | This is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2] | Domain |
EA [auth K] | PF00004 | ATPase 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] | PF16450 | Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C) | Proteasomal ATPase OB C-terminal domain | This is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2] | Domain |
FA [auth L] | PF17862 | AAA+ lid domain (AAA_lid_3) | AAA+ lid domain | This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. | Domain |
FA [auth L] | PF00004 | ATPase 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] | PF16450 | Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C) | Proteasomal ATPase OB C-terminal domain | This is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2] | Domain |
GA [auth M] | PF17862 | AAA+ lid domain (AAA_lid_3) | AAA+ lid domain | This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. | Domain |
GA [auth M] | PF00004 | ATPase 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 |
HA [auth J] | PF16450 | Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C) | Proteasomal ATPase OB C-terminal domain | This is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2] | Domain |
HA [auth J] | PF17862 | AAA+ lid domain (AAA_lid_3) | AAA+ lid domain | This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains. | Domain |
HA [auth J] | PF00004 | ATPase 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 |