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 22-FEB-2023, entry version 87. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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; PROTEASOME SUBUNIT ALPHA/BETA; 1. DR PANTHER; PTHR11599:SF6; PROTEASOME SUBUNIT BETA TYPE-2; 1. DR Pfam; PF00227; Proteasome; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 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 //