ID   PSB2_TRYBB              Reviewed;         206 AA.
AC   Q9NHC6;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Proteasome subunit beta type-2;
DE   AltName: Full=20S proteasome subunit beta-4;
GN   Name=PSB4;
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; AF226673; AAF37284.1; -; mRNA.
DR   AlphaFoldDB; Q9NHC6; -.
DR   SMR; Q9NHC6; -.
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:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR   GO; GO:0004175; F:endopeptidase activity; TAS:GeneDB.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISM:GeneDB.
DR   CDD; cd03758; proteasome_beta_type_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR035206; Proteasome_beta2.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF6; PTHR11599:SF6; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome.
FT   CHAIN           1..206
FT                   /note="Proteasome subunit beta type-2"
FT                   /id="PRO_0000148048"
SQ   SEQUENCE   206 AA;  22758 MW;  66A7400FECBE1BAB CRC64;
     MAETTIGFRC QDFVLVAAAG LNAFYYIKIT DTEDKITELD SHKVVACAGE NGPRTHFVEY
     VKCNMALKKM REHGRMISTH ATASFMRNTL AGALRSRDGL YPVNCLLAGF DVPASAEDDV
     ATGAHLYYLD YLGTLQEVPY GCHGYGAPFV TAMLDRMWRP NLTAQEGVEL MQKCCDEVNK
     RVVVSNNTFI CKAVPKDGVE RVQSVS