ID I1IKE1_BRADI Unreviewed; 237 AA.
AC I1IKE1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Proteasome subunit alpha type {ECO:0000256|RuleBase:RU000551};
GN Name=100836191 {ECO:0000313|EnsemblPlants:KQJ87824};
GN ORFNames=BRADI_4g13740v3 {ECO:0000313|EMBL:KQJ87824.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQJ87824};
RN [1] {ECO:0000313|EMBL:KQJ87824.1, ECO:0000313|EnsemblPlants:KQJ87824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ87824.1,
RC ECO:0000313|EnsemblPlants:KQJ87824};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ87824.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ87824.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ87824}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ87824};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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 EMBL; CM000883; KQJ87824.1; -; Genomic_DNA.
DR RefSeq; XP_003577362.1; XM_003577314.3.
DR AlphaFoldDB; I1IKE1; -.
DR STRING; 15368.I1IKE1; -.
DR EnsemblPlants; KQJ87824; KQJ87824; BRADI_4g13740v3.
DR GeneID; 100836191; -.
DR Gramene; KQJ87824; KQJ87824; BRADI_4g13740v3.
DR KEGG; bdi:100836191; -.
DR eggNOG; KOG0176; Eukaryota.
DR HOGENOM; CLU_035750_4_2_1; -.
DR InParanoid; I1IKE1; -.
DR OMA; NHYFTYN; -.
DR OrthoDB; 166567at2759; -.
DR Proteomes; UP000008810; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IBA:GO_Central.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03753; proteasome_alpha_type_5; 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; IPR033812; Proteasome_alpha_type_5.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF247; PROTEASOME SUBUNIT ALPHA TYPE; 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|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:UP000008810}.
FT DOMAIN 8..30
FT /note="Proteasome alpha-type subunits"
FT /evidence="ECO:0000259|PROSITE:PS00388"
SQ SEQUENCE 237 AA; 25895 MW; 2F9E8CB1CFCA248F CRC64;
MFLTRTEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGL KTKDGVVLAV EKRVTSPLLE
PSSVEKIMEI DEHVGCAMSG LIADARTLVE HARVETQNHR FSYGEPMTVE STTQAICDLA
LRFGEGDEES MSRPFGVSLL IAGHDENGPS LYYTDPSGTF WQCNAKAIGS GSEGADSSLQ
EQYNKELTLA EAETIALSIL KQVMEEKVTP NNVDIAKVSP SYHLYTPAEV EAVIARL
//
