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O28303 (PAN_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome-activating nucleotidase

Short name=PAN
Alternative name(s):
Proteasomal ATPase
Proteasome regulatory ATPase
Proteasome regulatory particle
Gene names
Name:pan
Ordered Locus Names:AF_1976
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceEvidence 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 HAMAP-Rule MF_00553.

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 componentCytoplasm
Proteasome
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteasomal protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein unfolding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteasome-activating nucleotidase complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

ATPase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Proteasome-activating nucleotidase HAMAP-Rule MF_00553
PRO_0000084739

Regions

Nucleotide binding185 – 1906ATP By similarity
Region396 – 3983Docks into pockets in the proteasome alpha-ring to cause gate opening By similarity
Coiled coil3 – 6058 Potential

Sites

Binding site3241ATP By similarity

Secondary structure

.............. 398
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O28303 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F3293BB7D6A646B4

FASTA39844,964
        10         20         30         40         50         60 
MGDSEIQYLL EKLKKLEEDY YKLRELYRRL EDEKKFIESE RIRYEREVRR LRSEVERLRS 

        70         80         90        100        110        120 
PPLLVGVVSD ILEDGRVVVK SSTGPKFVVN TSQYINEEEL KPGARVALNQ QTLAIVNVLP 

       130        140        150        160        170        180 
TSKDPMVYGF EVEEKPEVSY EDIGGLDVQI EEIREAVELP LLKPELFAEV GIEPPKGVLL 

       190        200        210        220        230        240 
YGPPGTGKTL LAKAVANQTR ATFIRVVGSE FVQKYIGEGA RLVREVFQLA KEKAPSIIFI 

       250        260        270        280        290        300 
DELDAIAARR TNSDTSGDRE VQRTMMQLLA ELDGFDPRGD VKVIGATNRI DILDPAILRP 

       310        320        330        340        350        360 
GRFDRIIEVP LPTFEGRIQI FKIHTRKMKL AEDVDFKELA RITEGASGAD IKAICTEAGM 

       370        380        390 
FAIREERAKV TMLDFTKAIE KVLKKTTPIP DLKGVMFV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000782 Genomic DNA. Translation: AAB89280.1.
PIRG69496.
RefSeqNP_070800.1. NC_000917.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WG5X-ray2.10A/B/C/D/E/F/G/H/I/J/K/L57-134[»]
2WG6X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L57-134[»]
ProteinModelPortalO28303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224325.AF1976.

Proteomic databases

PRIDEO28303.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB89280; AAB89280; AF_1976.
GeneID1485198.
KEGGafu:AF1976.

Phylogenomic databases

eggNOGCOG1222.
KOK03420.
OMAEREVNRT.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-2013-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00553. PAN.
InterProIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR023501. Nucleotidase_PAN.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00004. AAA. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01242. 26Sp45. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO28303.

Entry information

Entry namePAN_ARCFU
AccessionPrimary (citable) accession number: O28303
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references