ID   PSA_THESM               Reviewed;         260 AA.
AC   C6A459;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Proteasome subunit alpha {ECO:0000255|HAMAP-Rule:MF_00289};
DE   AltName: Full=20S proteasome alpha subunit {ECO:0000255|HAMAP-Rule:MF_00289};
DE   AltName: Full=Proteasome core protein PsmA {ECO:0000255|HAMAP-Rule:MF_00289};
GN   Name=psmA {ECO:0000255|HAMAP-Rule:MF_00289}; OrderedLocusNames=TSIB_1352;
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739;
RX   PubMed=19447963; DOI=10.1128/aem.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(2009).
CC   -!- FUNCTION: Component of the proteasome core, a large protease complex
CC       with broad specificity involved in protein degradation.
CC       {ECO:0000255|HAMAP-Rule:MF_00289}.
CC   -!- ACTIVITY REGULATION: The formation of the proteasomal ATPase PAN-20S
CC       proteasome complex, via the docking of the C-termini of PAN into the
CC       intersubunit pockets in the alpha-rings, triggers opening of the gate
CC       for substrate entry. Interconversion between the open-gate and close-
CC       gate conformations leads to a dynamic regulation of the 20S proteasome
CC       proteolysis activity. {ECO:0000255|HAMAP-Rule:MF_00289}.
CC   -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14 beta
CC       subunits that assemble into four stacked heptameric rings, resulting in
CC       a barrel-shaped structure. The two inner rings, each composed of seven
CC       catalytic beta subunits, are sandwiched by two outer rings, each
CC       composed of seven alpha subunits. The catalytic chamber with the active
CC       sites is on the inside of the barrel. Has a gated structure, the ends
CC       of the cylinder being occluded by the N-termini of the alpha-subunits.
CC       Is capped at one or both ends by the proteasome regulatory ATPase, PAN.
CC       {ECO:0000255|HAMAP-Rule:MF_00289}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|HAMAP-
CC       Rule:MF_00289}.
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DR   EMBL; CP001463; ACS90404.1; -; Genomic_DNA.
DR   RefSeq; WP_015849622.1; NC_012883.1.
DR   AlphaFoldDB; C6A459; -.
DR   SMR; C6A459; -.
DR   STRING; 604354.TSIB_1352; -.
DR   MEROPS; T01.970; -.
DR   EnsemblBacteria; ACS90404; ACS90404; TSIB_1352.
DR   GeneID; 8096353; -.
DR   KEGG; tsi:TSIB_1352; -.
DR   eggNOG; arCOG00971; Archaea.
DR   HOGENOM; CLU_035750_4_1_2; -.
DR   OMA; FQVEYAR; -.
DR   OrthoDB; 57654at2157; -.
DR   Proteomes; UP000009079; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03756; proteasome_alpha_archeal; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00289_A; Proteasome_A_A; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR019982; Proteasome_asu_arc.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR03633; arc_protsome_A; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Proteasome; Reference proteome.
FT   CHAIN           1..260
FT                   /note="Proteasome subunit alpha"
FT                   /id="PRO_1000204866"
FT   REGION          241..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   260 AA;  28882 MW;  1FA0506470D76CC2 CRC64;
     MAFVPPQAGY DRAITVFSPD GRLFQVQYAR EAVKRGATAV GVKCKDGVVL AVEKRVTSKL
     IEPESYEKIF QIDDHIAAAS SGIIADARVL VDRARLEAQI YRLTYGEPVP LTVLVKKICD
     LKQMHTQYGG VRPFGAALLM AGVNEKPELF ETDPSGAYFE WKAVAIGSGR NTAMAIFEEK
     YRDEMTLEEA IKLAVLALSK IMEEPSPESI EVAVISVKEK KFKKITPEEV AKCLEEALKE
     VEAEEVPEKE EDYSELDSNY