O28303 (PAN_ARCFU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Proteasome-activating nucleotidase Short name=PAN Alternative name(s): Proteasomal ATPase Proteasome regulatory ATPase Proteasome regulatory particle | ||||
| Gene names |
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| Organism | Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 224325 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus › ![]() |
Protein attributes
| Sequence length | 398 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates Probable. Ref.2 |
| Subunit structure | Homohexamer. The hexameric complex has a two-ring architecture resembling a top hat that caps the 20S proteasome core at one or both ends. Upon ATP-binding, the C-terminus of PAN interacts with the alpha-rings of the proteasome core by binding to the intersubunit pockets Probable. Ref.2 |
| Subcellular location | Cytoplasm By similarity. |
| Domain | Consists of three main regions, an N-terminal coiled-coil domain that may assist in substrate recognition, an interdomain involved in PAN hexamerization, and a C-terminal ATPase domain of the AAA type By similarity. HAMAP-Rule MF_00553 |
| Sequence similarities | Belongs to the AAA ATPase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Proteasome |
| Domain | Coiled coil |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Chaperone |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | ATP catabolic process Inferred from electronic annotation. Source: GOC proteasomal protein catabolic processInferred from electronic annotation. Source: HAMAP protein unfoldingInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome-activating nucleotidase complexInferred from electronic annotation. Source: HAMAP |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP ATPase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||
Molecule processing | ||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 398 | 398 | Proteasome-activating nucleotidase HAMAP-Rule MF_00553 | PRO_0000084739 | ||||||||||||||||||
Regions | ||||||||||||||||||||||
| Nucleotide binding | 185 – 190 | 6 | ATP By similarity | |||||||||||||||||||
| Region | 396 – 398 | 3 | Docks into pockets in the proteasome alpha-ring to cause gate opening By similarity | |||||||||||||||||||
| Coiled coil | 3 – 60 | 58 | Potential | |||||||||||||||||||
Sites | ||||||||||||||||||||||
| Binding site | 324 | 1 | ATP By similarity | |||||||||||||||||||
Secondary structure | ||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||
| Beta strand | 63 – 71 | 9 | ||||||||||||||||||||
| Beta strand | 77 – 81 | 5 | ||||||||||||||||||||
| Beta strand | 86 – 89 | 4 | ||||||||||||||||||||
| Turn | 97 – 99 | 3 | ||||||||||||||||||||
| Beta strand | 105 – 109 | 5 | ||||||||||||||||||||
| Turn | 110 – 112 | 3 | ||||||||||||||||||||
| Beta strand | 115 – 119 | 5 | ||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. Venter J.C.Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126. |
| [2] | "Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases." Djuranovic S., Hartmann M.D., Habeck M., Ursinus A., Zwickl P., Martin J., Lupas A.N., Zeth K. Mol. Cell 34:580-590(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 57-134 OF WILD-TYPE AND MUTANT ALA-61, FUNCTION AS A CHAPERONE, SUBUNIT. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE000782 Genomic DNA. Translation: AAB89280.1. | ||||||||||||||||||
| PIR | G69496. | ||||||||||||||||||
| RefSeq | NP_070800.1. NC_000917.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | O28303. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | 224325.AF1976. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | O28303. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| EnsemblBacteria | AAB89280; AAB89280; AF_1976. | ||||||||||||||||||
| GeneID | 1485198. | ||||||||||||||||||
| KEGG | afu:AF1976. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | COG1222. | ||||||||||||||||||
| KO | K03420. | ||||||||||||||||||
| OMA | RVNERKA. | ||||||||||||||||||
| ProtClustDB | PRK03992. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | AFUL224325:GJBC-2013-MONOMER. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| HAMAP | MF_00553. PAN. | ||||||||||||||||||
| InterPro | IPR005937. 26S_Psome_P45. IPR003593. AAA+_ATPase. IPR003959. ATPase_AAA_core. IPR003960. ATPase_AAA_CS. IPR023501. Nucleotidase_PAN. [Graphical view] | ||||||||||||||||||
| Pfam | PF00004. AAA. 1 hit. [Graphical view] | ||||||||||||||||||
| SMART | SM00382. AAA. 1 hit. [Graphical view] | ||||||||||||||||||
| TIGRFAMs | TIGR01242. 26Sp45. 1 hit. | ||||||||||||||||||
| PROSITE | PS00674. AAA. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | O28303. | ||||||||||||||||||
Entry information
| Entry name | PAN_ARCFU | ||||||||
| Accession | Primary (citable) accession number: O28303 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
