3JTL
Crystal structure of archaeal 20S proteasome in complex with mutated P26 activator
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
B | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034248 | 3000131 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034248 | 3000131 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034248 | 3000131 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034248 | 3000131 | SCOP2B (2022-06-29) |
E | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034248 | 3000131 | SCOP2B (2022-06-29) |
F | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034248 | 3000131 | SCOP2B (2022-06-29) |
G | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034248 | 3000131 | SCOP2B (2022-06-29) |
H | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034254 | 3000131 | SCOP2B (2022-06-29) |
J | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034254 | 3000131 | SCOP2B (2022-06-29) |
K | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034254 | 3000131 | SCOP2B (2022-06-29) |
M | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034254 | 3000131 | SCOP2B (2022-06-29) |
N | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034254 | 3000131 | SCOP2B (2022-06-29) |
I | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034254 | 3000131 | SCOP2B (2022-06-29) |
L | SCOP2B Superfamily | Class II glutamine amidotransferases | 8034254 | 3000131 | SCOP2B (2022-06-29) |
P | SCOP2B Superfamily | Proteasome activator-like | 8032475 | 3001611 | SCOP2B (2022-06-29) |
R | SCOP2B Superfamily | Proteasome activator-like | 8032475 | 3001611 | SCOP2B (2022-06-29) |
S | SCOP2B Superfamily | Proteasome activator-like | 8032475 | 3001611 | SCOP2B (2022-06-29) |
T | SCOP2B Superfamily | Proteasome activator-like | 8032475 | 3001611 | SCOP2B (2022-06-29) |
U | SCOP2B Superfamily | Proteasome activator-like | 8032475 | 3001611 | SCOP2B (2022-06-29) |
O | SCOP2B Superfamily | Proteasome activator-like | 8032475 | 3001611 | SCOP2B (2022-06-29) |
Q | SCOP2B Superfamily | Proteasome activator-like | 8032475 | 3001611 | 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) |
---|---|---|---|---|---|---|---|---|
B | PF00227,PF10584 | e3jtlB1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
D | PF00227,PF10584 | e3jtlD1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
A | PF00227,PF10584 | e3jtlA1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
C | PF00227,PF10584 | e3jtlC1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
E | PF00227,PF10584 | e3jtlE1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
F | PF00227,PF10584 | e3jtlF1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
G | PF00227,PF10584 | e3jtlG1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227,PF10584 | ECOD (1.6) |
H | PF00227 | e3jtlH1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
J | PF00227 | e3jtlJ1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
K | PF00227 | e3jtlK1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
M | PF00227 | e3jtlM1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
N | PF00227 | e3jtlN1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
I | PF00227 | e3jtlI1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
L | PF00227 | e3jtlL1 | A: a+b four layers | X: Ntn/PP2C | H: Ntn | T: Proteasome subunits | F: PF00227 | ECOD (1.6) |
P | PF02252 | e3jtlP1 | A: alpha bundles | X: Four-helical up-and-down bundle | H: Proteasome activator reg(alpha) (From Topology) | T: Proteasome activator reg(alpha) | F: PF02252 | ECOD (1.6) |
R | PF02252 | e3jtlR1 | A: alpha bundles | X: Four-helical up-and-down bundle | H: Proteasome activator reg(alpha) (From Topology) | T: Proteasome activator reg(alpha) | F: PF02252 | ECOD (1.6) |
S | PF02252 | e3jtlS1 | A: alpha bundles | X: Four-helical up-and-down bundle | H: Proteasome activator reg(alpha) (From Topology) | T: Proteasome activator reg(alpha) | F: PF02252 | ECOD (1.6) |
T | PF02252 | e3jtlT1 | A: alpha bundles | X: Four-helical up-and-down bundle | H: Proteasome activator reg(alpha) (From Topology) | T: Proteasome activator reg(alpha) | F: PF02252 | ECOD (1.6) |
U | PF02252 | e3jtlU1 | A: alpha bundles | X: Four-helical up-and-down bundle | H: Proteasome activator reg(alpha) (From Topology) | T: Proteasome activator reg(alpha) | F: PF02252 | ECOD (1.6) |
O | PF02252 | e3jtlO1 | A: alpha bundles | X: Four-helical up-and-down bundle | H: Proteasome activator reg(alpha) (From Topology) | T: Proteasome activator reg(alpha) | F: PF02252 | ECOD (1.6) |
Q | PF02252 | e3jtlQ1 | A: alpha bundles | X: Four-helical up-and-down bundle | H: Proteasome activator reg(alpha) (From Topology) | T: Proteasome activator reg(alpha) | F: PF02252 | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
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 | |
PF10584 | Proteasome subunit A N-terminal signature (Proteasome_A_N) | Proteasome subunit A N-terminal signature | - | Family | |
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 | |
PF02252 | Proteasome activator pa28 beta subunit (PA28_beta) | Proteasome activator pa28 beta subunit | - | Family |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR000426 | Proteasome alpha-subunit, N-terminal domain | Domain | |
IPR029055 | Nucleophile aminohydrolases, N-terminal | Homologous Superfamily | |
IPR023332 | Proteasome alpha-type subunit | Family | |
IPR001353 | Proteasome, subunit alpha/beta | Family | |
IPR019982 | Proteasome alpha subunit, archaeal | Family | |
IPR016050 | Proteasome beta-type subunit, conserved site | Conserved Site | |
IPR023333 | Proteasome B-type subunit | Family | |
IPR029055 | Nucleophile aminohydrolases, N-terminal | Homologous Superfamily | |
IPR019983 | Peptidase T1A, proteasome beta-subunit, archaeal | Family | |
IPR001353 | Proteasome, subunit alpha/beta | Family | |
IPR000243 | Peptidase T1A, proteasome beta-subunit | Family | |
IPR003186 | Proteasome activator PA28, C-terminal domain | Domain | |
IPR036252 | Proteasome activator superfamily | Homologous Superfamily | |
IPR036997 | Proteasome activator PA28, C-terminal domain superfamily | Homologous Superfamily |