ID M0MJA8_9EURY Unreviewed; 245 AA.
AC M0MJA8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Proteasome subunit alpha {ECO:0000256|HAMAP-Rule:MF_00289, ECO:0000256|RuleBase:RU000552};
DE AltName: Full=20S proteasome alpha subunit {ECO:0000256|HAMAP-Rule:MF_00289};
DE AltName: Full=Proteasome core protein PsmA {ECO:0000256|HAMAP-Rule:MF_00289};
GN Name=psmA {ECO:0000256|HAMAP-Rule:MF_00289};
GN ORFNames=C449_07460 {ECO:0000313|EMBL:EMA45443.1};
OS Halococcus saccharolyticus DSM 5350.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1227455 {ECO:0000313|EMBL:EMA45443.1, ECO:0000313|Proteomes:UP000011669};
RN [1] {ECO:0000313|EMBL:EMA45443.1, ECO:0000313|Proteomes:UP000011669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5350 {ECO:0000313|EMBL:EMA45443.1,
RC ECO:0000313|Proteomes:UP000011669};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Component of the proteasome core, a large protease complex
CC with broad specificity involved in protein degradation.
CC {ECO:0000256|HAMAP-Rule:MF_00289, ECO:0000256|RuleBase:RU000552}.
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:0000256|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:0000256|HAMAP-Rule:MF_00289, ECO:0000256|RuleBase:RU000552}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00289, ECO:0000256|RuleBase:RU000552}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|HAMAP-
CC Rule:MF_00289, ECO:0000256|PROSITE-ProRule:PRU00808,
CC ECO:0000256|RuleBase:RU000552}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMA45443.1}.
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DR EMBL; AOMD01000018; EMA45443.1; -; Genomic_DNA.
DR RefSeq; WP_006077348.1; NZ_AOMD01000018.1.
DR AlphaFoldDB; M0MJA8; -.
DR STRING; 1227455.C449_07460; -.
DR PATRIC; fig|1227455.4.peg.1524; -.
DR InParanoid; M0MJA8; -.
DR OrthoDB; 9421at2157; -.
DR Proteomes; UP000011669; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
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; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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 NCBIfam; TIGR03633; arc_protsome_A; 1.
DR PANTHER; PTHR11599:SF15; PROTEASOME SUBUNIT ALPHA TYPE-7-1-RELATED; 1.
DR PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00289};
KW Hydrolase {ECO:0000313|EMBL:EMA45443.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|HAMAP-
KW Rule:MF_00289}; Reference proteome {ECO:0000313|Proteomes:UP000011669}.
FT DOMAIN 10..32
FT /note="Proteasome alpha-type subunits"
FT /evidence="ECO:0000259|PROSITE:PS00388"
SQ SEQUENCE 245 AA; 26792 MW; F4E2297F245806C5 CRC64;
MQGQNQQQAY DRGTTIFSPD GRLYQVEYAR EAVERGSPSL GVRTEDGVVL VAEQRVRSPL
MEQSSIEKLH KVDDHIAVGS AGHVADARQL TDFARQQAQV DRLRYGEPIG VETLAGAVTD
HIQEYTQTGG ARPFGVSLLI AGVEDGEPRL FETDPSGTAT EWAASAVGAD REAIHDSLET
NYRADADLDG GIDTALRALA SVRDAFEPSE VTIATIDVET EQYRTLDDDE IEAHLDEIDF
EDDDE
//
