ID A0A1I2X025_9EURY Unreviewed; 271 AA.
AC A0A1I2X025;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=SAMN04488063_0076 {ECO:0000313|EMBL:SFH06898.1};
OS Halopelagius inordinatus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=553467 {ECO:0000313|EMBL:SFH06898.1, ECO:0000313|Proteomes:UP000198876};
RN [1] {ECO:0000313|Proteomes:UP000198876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7739 {ECO:0000313|Proteomes:UP000198876};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FOOQ01000012; SFH06898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2X025; -.
DR STRING; 553467.SAMN04488063_0076; -.
DR Proteomes; UP000198876; 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 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 PANTHER; PTHR11599:SF15; PROTEASOME SUBUNIT ALPHA TYPE-7-1-RELATED; 1.
DR PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR Pfam; PF00227; Proteasome; 2.
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 Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|HAMAP-
KW Rule:MF_00289}; Reference proteome {ECO:0000313|Proteomes:UP000198876}.
FT DOMAIN 17..39
FT /note="Proteasome alpha-type subunits"
FT /evidence="ECO:0000259|PROSITE:PS00388"
FT REGION 135..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 271 AA; 29376 MW; 59CE68CD5EFFE441 CRC64;
MLGSEVYTMN RNDQQAYDRG TSLFSPDGRI YQVEYAREAV KRGASSVGVR TADGVVLAAQ
RRTSSNLMET ESIEKLHKLD EFLGAASAGH VADARQLVDD ARTEAQRNRL RYGEPLGVET
LTKTLSDQIQ ESTQIGGTRP FGASLLIGGV DGDVGRPSPP AREADSDEGR DVRPRLFQTD
PSGAPQEWKA VAIGSNRGDI QEFLEDEWNE DISVDDGVTL AIRALLVGED DLTAEEIAIS
TISAEGYHQV EDDDVSAIIE EFGGSGDDDE E
//
