ID Q8IJT1_PLAF7 Unreviewed; 271 AA. AC Q8IJT1; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 02-OCT-2007, entry version 28. DE Proteasome subunit beta type (EC 3.4.25.1). GN ORFNames=PF10_0111; OS Plasmodium falciparum (isolate 3D7). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=36329; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=3D7; RX MEDLINE=22255705; PubMed=12368864; DOI=10.1038/nature01097; RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K., RA Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., RA Chan M.-S., Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., RA Pertea M., Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., RA Martin D.M.A., Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., RA McFadden G.I., Cummings L.M., Subramanian G.M., Mungall C., RA Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., Davis R.W., RA Fraser C.M., Barrell B.G.; RT "Genome sequence of the human malaria parasite Plasmodium RT falciparum."; RL Nature 419:498-511(2002). CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex CC which is characterized by its ability to cleave peptides with Arg, CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or CC slightly basic pH. The proteasome has an ATP-dependent proteolytic CC activity (By similarity). CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. CC -!- SUBUNIT: The proteasome is composed of at least 15 non identical CC subunits which form a highly ordered ring-shaped structure (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity). CC -!- SIMILARITY: Belongs to the peptidase T1B family. 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; AE014830; AAN35309.1; -; Genomic_DNA. DR RefSeq; XP_001347396.1; -. DR HSSP; P30656; 1G0U. DR MEROPS; T01.012; -. DR GeneID; 810269; -. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-KW. DR GO; GO:0005839; C:proteasome core complex (sensu Eukaryota); IEA:InterPro. DR GO; GO:0004298; F:threonine endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR InterPro; IPR000243; Pept_T1A_subB. DR InterPro; IPR001353; Proteasome_A_B. DR Pfam; PF00227; Proteasome; 1. DR PRINTS; PR00141; PROTEASOME. DR PROSITE; PS00854; PROTEASOME_B; 1. PE 3: Inferred from homology; KW Cytoplasm; Hydrolase; Protease; Proteasome; Threonine protease. SQ SEQUENCE 271 AA; 30596 MW; CBDA4F07503EB4E3 CRC64; MVIASDESFM NEIDNLINDV EDERIDNDEL EFCVAPVNVP RNFIKYAQTQ NKKLFDFHKG TTTLAFKFKD GIIVAVDSRA SMGSFISSQN VEKIIEINKN ILGTMAGGAA DCLYWEKYLG KIIKIYELRN NEKISVRAAS TILSNILYQY KGYGLCCGII LSGYDHTGFN MFYVDDSGKK VEGNLFSCGS GSTYAYSILD SAYDYNLNLD QAVELARNAI YHATFRDGGS GGKVRVFHIH KNGYDKIIEG EDVFDLHYHY TNPEQKDQYV M //