ID A0A0E0JV73_ORYPU Unreviewed; 270 AA.
AC A0A0E0JV73;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Proteasome subunit alpha type {ECO:0000256|RuleBase:RU000551};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC02G02090.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC02G02090.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC02G02090.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity.
CC {ECO:0000256|ARBA:ARBA00002000}.
CC -!- SUBUNIT: The 20S proteasome core is composed of 28 subunits that are
CC arranged in four stacked rings, resulting in a barrel-shaped structure.
CC The two end rings are each formed by seven alpha subunits, and the two
CC central rings are each formed by seven beta subunits.
CC {ECO:0000256|RuleBase:RU000551}.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. {ECO:0000256|ARBA:ARBA00026071}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000551}.
CC Nucleus {ECO:0000256|RuleBase:RU000551}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC ProRule:PRU00808, ECO:0000256|RuleBase:RU000551}.
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DR AlphaFoldDB; A0A0E0JV73; -.
DR STRING; 4537.A0A0E0JV73; -.
DR EnsemblPlants; OPUNC02G02090.1; OPUNC02G02090.1; OPUNC02G02090.
DR Gramene; OPUNC02G02090.1; OPUNC02G02090.1; OPUNC02G02090.
DR eggNOG; KOG0863; Eukaryota.
DR HOGENOM; CLU_035750_8_0_1; -.
DR OMA; LNCKAMA; -.
DR Proteomes; UP000026962; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03749; proteasome_alpha_type_1; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR035144; Proteasome_alpha1.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF12; PROTEASOME SUBUNIT ALPHA TYPE-1; 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|RuleBase:RU000551};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000551};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW ProRule:PRU00808}; Reference proteome {ECO:0000313|Proteomes:UP000026962}.
FT DOMAIN 6..28
FT /note="Proteasome alpha-type subunits"
FT /evidence="ECO:0000259|PROSITE:PS00388"
FT REGION 239..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 270 AA; 29601 MW; 2A392B5FC6588900 CRC64;
MFRNQYDTDV TTWSPAGRLF QVEYAMEAVK QGSACVGLRS RTHAVLAAAN KAASELSSHQ
RKVFRVADHA GVALAGLTAD GRVLSRFLRS ECINHAFVYD APLPVSRLAL RLADKAQVCT
QRSWKRPYGV GLLVAGLDES GAHLYYNCPS GNYFEYQAFA IGSRSQAAKT FLERRFEGYN
DYTPEQLIKD ALSAIKETLQ GEKLTSSNCT VAIVGRKDDG TVEPFEMIDA KRIQEIINSM
EAAEEAPAAE AESSSMQEED KGTDAAPMDI
//
