ID   PSA1_HALMA              Reviewed;         260 AA.
AC   Q5V2X8;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Proteasome subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_00289};
DE   AltName: Full=20S proteasome alpha subunit 1 {ECO:0000255|HAMAP-Rule:MF_00289};
DE   AltName: Full=Proteasome core protein PsmA 1 {ECO:0000255|HAMAP-Rule:MF_00289};
GN   Name=psmA1 {ECO:0000255|HAMAP-Rule:MF_00289}; OrderedLocusNames=rrnAC1174;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV46124.1; -; Genomic_DNA.
DR   RefSeq; WP_004960819.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V2X8; -.
DR   SMR; Q5V2X8; -.
DR   STRING; 272569.rrnAC1174; -.
DR   EnsemblBacteria; AAV46124; AAV46124; rrnAC1174.
DR   GeneID; 40152169; -.
DR   GeneID; 64822204; -.
DR   KEGG; hma:rrnAC1174; -.
DR   PATRIC; fig|272569.17.peg.1890; -.
DR   eggNOG; arCOG00971; Archaea.
DR   HOGENOM; CLU_035750_4_1_2; -.
DR   OMA; FQVEYAR; -.
DR   Proteomes; UP000001169; Chromosome I.
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; 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 1"
FT                   /id="PRO_0000124168"
FT   REGION          237..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..260
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   260 AA;  28383 MW;  A3AE52D6CDE15672 CRC64;
     MQGQNQQQAY DRGITIFSPD GRLYQVEYAR EAVKRGTASI GVRTSDGVVL AVDKRIRSPL
     MERSSVEKIH KADDHIGIAS AGHVADARQL IDFARRQAQV NQLRYGEPVG VETLTKEITD
     YIQQYTQVGG ARPFGVALII GGIVNGEPRL FETDPSGTPY EWKALAVGAD RGDIRDYLEE
     HYDEGMDLDE GVDLALAALA SVNDDELSPE GIGVATVDVE TETFGQLTDE EKEAHLAEAD
     LLDTGEDADD EAEDEDATEE