ID   PSA_THEKO               Reviewed;         260 AA.
AC   Q5JIU9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 109.
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=TK1637;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP006878; BAD85826.1; -; Genomic_DNA.
DR   RefSeq; WP_011250588.1; NC_006624.1.
DR   AlphaFoldDB; Q5JIU9; -.
DR   SMR; Q5JIU9; -.
DR   IntAct; Q5JIU9; 1.
DR   MINT; Q5JIU9; -.
DR   STRING; 69014.TK1637; -.
DR   EnsemblBacteria; BAD85826; BAD85826; TK1637.
DR   GeneID; 3235074; -.
DR   KEGG; tko:TK1637; -.
DR   PATRIC; fig|69014.16.peg.1596; -.
DR   eggNOG; arCOG00971; Archaea.
DR   HOGENOM; CLU_035750_4_1_2; -.
DR   InParanoid; Q5JIU9; -.
DR   OMA; FQVEYAR; -.
DR   OrthoDB; 57654at2157; -.
DR   PhylomeDB; Q5JIU9; -.
DR   Proteomes; UP000000536; 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..260
FT                   /note="Proteasome subunit alpha"
FT                   /id="PRO_0000124185"
SQ   SEQUENCE   260 AA;  29211 MW;  76CAB65E6B6E7D03 CRC64;
     MAFVPPQAGY DRAITVFSPD GRLFQVNYAR EAVKRGATAV GVKWKDGVVL AVEKRITSKL
     IEPSSYEKIF LIDDHIAAAP SGIIADARVL VDRARLEAQI YRLTYGEPVP LTVLVKKICD
     LKQAHTQYGG VRPFGAALLM AGVNEKPELF ETDPSGAYFE WKAVAIGSGR NTAMAIFEEH
     YRDDIGKDDA IKLAILALAK TLEEPTAEGI EVAYITMDEK RWKKLPREEL EKYINEILQE
     VKEEEVEEKQ EDYSELDQNY