ID   PSB1_TRYBB              Reviewed;         258 AA.
AC   Q9U794;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Proteasome subunit beta type-1;
DE   AltName: Full=20S proteasome subunit beta-6;
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: Non-catalytic component of the proteasome, a multicatalytic
CC       proteinase complex which is characterized by its ability to cleave
CC       peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group
CC       at neutral or slightly basic pH. The proteasome has an ATP-dependent
CC       proteolytic activity (By similarity). {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU00809}.
CC       Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; AF148124; AAF05905.1; -; mRNA.
DR   AlphaFoldDB; Q9U794; -.
DR   SMR; Q9U794; -.
DR   BRENDA; 3.4.25.1; 6519.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR035202; Proteasome_beta1.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF59; PTHR11599:SF59; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome.
FT   CHAIN           1..258
FT                   /note="Proteasome subunit beta type-1"
FT                   /id="PRO_0000148037"
SQ   SEQUENCE   258 AA;  28716 MW;  AA72EB9FAD9D7383 CRC64;
     MIEDFSEHHV GEANTLQHHG YPRKLGNSVL TLPLRQGAKG HPQHWSPYTD NGGTIAAIAG
     SNYVVLGADT RLNGDFCIHT RSDTSKLFKL TDRIFLASSG MQADRLQLQQ MLKYRIQWYQ
     YNNGGKVPST KAIAKLTSTM LYQRRFFPYY TFNMIVGIDE KGAGVCYSYD PVGSTEPFRY
     GTCGSASSFV EPLLDCLLTR QHMVTQAPAD LTMEEALGML KNAFTGAAER DIFTGDTVCF
     HIITADGVGT EMFELRKD