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C3MVG1 (PSA_SULIM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 36. 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:M1425_1403
OrganismSulfolobus islandicus (strain M.14.25 / Kamchatka #1) [Complete proteome] [HAMAP]
Taxonomic identifier427317 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length241 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 – 241241Proteasome subunit alpha HAMAP-Rule MF_00289
PRO_1000204862

Sequences

Sequence LengthMass (Da)Tools
C3MVG1 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: EBF7FFEB124FF85D

FASTA24126,535
        10         20         30         40         50         60 
MAFGPAAMGY DRAITIFSPD GSLYQVDYAF EAVKKGWTAI GIKSKSGVVI ASEKRKAQSL 

        70         80         90        100        110        120 
LDVDSIEKVF LIDDHVGCSF AGLASDGRVL IDYARNIALQ HRLIYDEPVS IDYLTKSVAD 

       130        140        150        160        170        180 
VKQMYTQHGG VRPFGVALVI AGIDKSVPKL YMTEPSGQYM PYQAVAIGQG YYTATEFLEK 

       190        200        210        220        230        240 
NYKEDLTIED TILLALKALS ATLKPNEKLT PNTVEIGYAS TQTGLFLKMT SEDKNMYLQK 


L 

« Hide

References

[1]"Biogeography of the Sulfolobus islandicus pan-genome."
Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.
Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M.14.25 / Kamchatka #1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001400 Genomic DNA. Translation: ACP38156.1.
RefSeqYP_002829454.1. NC_012588.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING427317.M1425_1403.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP38156; ACP38156; M1425_1403.
GeneID7793851.
KEGGsia:M1425_1403.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091085.
KOK03432.
OMAFQVNYAR.

Enzyme and pathway databases

BioCycSISL427317:GI7C-1448-MONOMER.

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_SULIM
AccessionPrimary (citable) accession number: C3MVG1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: June 11, 2014
This is version 36 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