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Q9V122 (PSA_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 102. 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 subunit alpha

EC=3.4.25.1
Alternative name(s):
20S proteasome alpha subunit
Proteasome core protein PsmA
Gene names
Name:psmA
Ordered Locus Names:PYRAB06070
ORF Names:PAB0417
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation By similarity. HAMAP-Rule MF_00289

Catalytic activity

Cleavage of peptide bonds with very broad specificity. HAMAP-Rule MF_00289

Enzyme regulation

The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity By similarity. HAMAP-Rule MF_00289

Subunit structure

The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is capped at one or both ends by the proteasome regulatory ATPase, PAN By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00289.

Sequence similarities

Belongs to the peptidase T1A family.

Ontologies

Keywords
   Cellular componentCytoplasm
Proteasome
   Molecular functionHydrolase
Protease
Threonine protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteasome core complex, alpha-subunit complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionthreonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260Proteasome subunit alpha HAMAP-Rule MF_00289
PRO_0000124181

Sequences

Sequence LengthMass (Da)Tools
Q9V122 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 8551E62E245D37B4

FASTA26028,994
        10         20         30         40         50         60 
MAFVPPQAGY DRAITVFSPD GRLFQVNYAR EAVKRGATAV GVKCKDGVVL AVEKRITSRL 

        70         80         90        100        110        120 
IEPESYEKIF QIDDHIAAAS SGIIADARVL VNRARLEAQI HRLTYGEPAP LAVIVKKICD 

       130        140        150        160        170        180 
LKQMHTQYGG VRPFGAALLM AGVNDKPELY ETDPSGAYFA WKAVAIGSGR NTAMAIFEDK 

       190        200        210        220        230        240 
YRDDMTLDEA IKLAIFALAK TMEKPSAENI EVAVITVKDK KFRKLSKEEI EKFLGEVMKE 

       250        260 
VEEEEVKEKE EDYSELDSHY 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248284 Genomic DNA. Translation: CAB49529.1.
HE613800 Genomic DNA. Translation: CCE69999.1.
PIRB75181.
RefSeqNP_126298.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V122.
SMRQ9V122. Positions 6-238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB0417.

Protein family/group databases

MEROPST01.973.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB49529; CAB49529; PAB0417.
GeneID1495512.
KEGGpab:PAB0417.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091085.
KOK03432.
OMAFQVNYAR.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
HAMAPMF_00289_A. Proteasome_A_A.
InterProIPR029055. Ntn_hydrolases_N.
IPR019982. Proteasome_asu_arc.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR03633. arc_protsome_A. 1 hit.
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSA_PYRAB
AccessionPrimary (citable) accession number: Q9V122
Secondary accession number(s): G8ZJ72
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 102 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

Peptidase families

Classification of peptidase families and list of entries