ID   PSA7_TRYBB              Reviewed;         247 AA.
AC   Q9NDA2;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Proteasome subunit alpha type-7;
DE   AltName: Full=20S proteasome subunit alpha-4;
GN   Name=PSA4;
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; AF169652; AAF89684.1; -; mRNA.
DR   AlphaFoldDB; Q9NDA2; -.
DR   SMR; Q9NDA2; -.
DR   MEROPS; T01.974; -.
DR   PRIDE; Q9NDA2; -.
DR   BRENDA; 3.4.25.1; 6519.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0005829; C:cytosol; ISA:GeneDB.
DR   GO; GO:0005730; C:nucleolus; IDA:GeneDB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:GeneDB.
DR   GO; GO:0005634; C:nucleus; ISA:GeneDB.
DR   GO; GO:0005839; C:proteasome core complex; ISM:GeneDB.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
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   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..247
FT                   /note="Proteasome subunit alpha type-7"
FT                   /id="PRO_0000124158"
SQ   SEQUENCE   247 AA;  27865 MW;  B2C522510C068670 CRC64;
     MSYDRAITVF SPDGHLFQVE YAQEAVRKGL CAVGVKGKDS IIFAVEKKSV QKLQDSRTTR
     KIYKLDEHIY LASAGLSADA RVVVNHAQLE CQRFRLSYED AIDVDLLVRY VARVQQRSTQ
     SSGSRPYGVS TIIGGFNENG QPQLWKTEPS GTSSAWNAAA IGRNDKVVLE FMEKNYQDGM
     TRDRCVHFAI KALLEAVESG SKNIELLVLE RGKAAYMSDT ELHRFVVEVE KEREEEAARR
     RRLAEED