ID   PSA2_TRYBB              Reviewed;         231 AA.
AC   Q9U793;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Proteasome subunit alpha type-2;
DE   AltName: Full=20S proteasome subunit alpha-2;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=427;
RX   PubMed=11309374; DOI=10.1074/jbc.m008342200;
RA   Huang L., Jacob R.J., Pegg S.C.H., Baldwin M.A., Wang C.C.,
RA   Burlingame A.L., Babbitt P.C.;
RT   "Functional assignment of the 20 S proteasome from Trypanosoma brucei using
RT   mass spectrometry and new bioinformatics approaches.";
RL   J. Biol. Chem. 276:28327-28339(2001).
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   -!- 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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; AF148125; AAF05906.1; -; mRNA.
DR   AlphaFoldDB; Q9U793; -.
DR   SMR; Q9U793; -.
DR   OMA; YQEQIPT; -.
DR   BRENDA; 3.4.25.1; 6519.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0004175; F:endopeptidase activity; ISM:GeneDB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISM:GeneDB.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR034644; Proteasome_subunit_alpha2.
DR   PANTHER; PTHR11599:SF16; PTHR11599:SF16; 1.
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   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome.
FT   CHAIN           1..231
FT                   /note="Proteasome subunit alpha type-2"
FT                   /id="PRO_0000124084"
SQ   SEQUENCE   231 AA;  25355 MW;  80026D6FC40F8429 CRC64;
     MSESSYGLTT FSPSGRLVQI EYATTAASKG TTALGVKATD GVVIAAEKKT TSPLADSLTL
     HKVFALDDHV GCTYSGIGPD CRVLVDAARR ACQRYRLTYH EPMPISQLVR QISFLFQEFT
     QSGGVRPFGC SLLVAGADSR GNHLYQLDPS GTFWTWKATS IGKGSPDART FLEKRYTNEM
     EIEDAVHTAL LTLKEGFDGR MTAENTQVGR VVEGRFELLT VEQLKDYLDQ I