ID   PSA_PYRAE               Reviewed;         243 AA.
AC   Q8ZVM1;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 119.
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=PAE2215;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64035.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZVM1; -.
DR   SMR; Q8ZVM1; -.
DR   STRING; 178306.PAE2215; -.
DR   MEROPS; T01.970; -.
DR   EnsemblBacteria; AAL64035; AAL64035; PAE2215.
DR   KEGG; pai:PAE2215; -.
DR   PATRIC; fig|178306.9.peg.1647; -.
DR   eggNOG; arCOG00971; Archaea.
DR   HOGENOM; CLU_035750_4_1_2; -.
DR   InParanoid; Q8ZVM1; -.
DR   OMA; FQVEYAR; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
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; IBA:GO_Central.
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; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Proteasome; Reference proteome.
FT   CHAIN           1..243
FT                   /note="Proteasome subunit alpha"
FT                   /id="PRO_0000124182"
SQ   SEQUENCE   243 AA;  26626 MW;  53D9907408AA61A9 CRC64;
     MFPPAMAGYD RAITIFSPEG KIYQVEYAGE AVKRGWPTVG VKCKAGVVLT AEKRKISALF
     DSSSLEKIYL IDEHVAASPS GLLADARILI DYARDVALSH RFIYDEPIDV EFLTKAVCNL
     KQQYTQFGGA RPFGVALLIA GVDRHGARLY QTDPSGVYIG YFATAIGAES GTITEFLEKN
     YKFDMEMGEC IELALKALAS AVEITDSANV EVAYATIEEK KMRKMSQDEV ASLLTKLGLL
     KKS