ID Q8IJT1_PLAF7 Unreviewed; 271 AA. AC Q8IJT1; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 29-OCT-2014, entry version 86. DE RecName: Full=Proteasome subunit beta type {ECO:0000256|RuleBase:RU004203}; DE EC=3.4.25.1 {ECO:0000256|RuleBase:RU004203}; GN ORFNames=PF10_0111 {ECO:0000313|EMBL:AAN35309.1}; OS Plasmodium falciparum (isolate 3D7). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=36329 {ECO:0000313|EMBL:AAN35309.1, ECO:0000313|Proteomes:UP000001450}; RN [1] {ECO:0000313|EMBL:AAN35309.1, ECO:0000313|Proteomes:UP000001450} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450}; RX 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.; 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. {ECO:0000256|RuleBase:RU004203}. CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. {ECO:0000256|RuleBase:RU000694}. CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and CC two 19S regulatory subunits. The 20S proteasome core is composed CC of 28 subunits that are arranged in four stacked rings, resulting CC in a barrel-shaped structure. The two end rings are each formed by CC seven alpha subunits, and the two central rings are each formed by CC seven beta subunits. {ECO:0000256|RuleBase:RU004203}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000694, CC ECO:0000256|SAAS:SAAS00039306}. Nucleus CC {ECO:0000256|RuleBase:RU000694, ECO:0000256|SAAS:SAAS00039306}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. CC {ECO:0000256|RuleBase:RU004202}. 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; XM_001347360.1. DR ProteinModelPortal; Q8IJT1; -. DR SMR; Q8IJT1; 61-261. DR IntAct; Q8IJT1; 13. DR MINT; MINT-1554977; -. DR STRING; 5833.PF10_0111-1; -. DR MEROPS; T01.A15; -. DR EnsemblProtists; PF10_0111:mRNA; PF10_0111:pep; PF10_0111. DR GeneID; 810269; -. DR KEGG; pfa:PF10_0111; -. DR EuPathDB; PlasmoDB:PF3D7_1011400; -. DR HOGENOM; HOG000091082; -. DR InParanoid; Q8IJT1; -. DR KO; K02737; -. DR OMA; LRAIMHA; -. DR PhylomeDB; Q8IJT1; -. DR Reactome; REACT_192628; AUF1 (hnRNP D0) destabilizes mRNA. DR Reactome; REACT_192689; ER-Phagosome pathway. DR Reactome; REACT_192695; Antigen processing: Ubiquitination & Proteasome degradation. DR Reactome; REACT_192713; Cross-presentation of soluble exogenous antigens (endosomes). DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB_Pfalciparum. DR GO; GO:0005634; C:nucleus; IDA:GeneDB_Pfalciparum. DR GO; GO:0005839; C:proteasome core complex; ISS:GeneDB_Pfalciparum. DR GO; GO:0004175; F:endopeptidase activity; ISS:GeneDB_Pfalciparum. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:GeneDB_Pfalciparum. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR000243; Pept_T1A_subB. DR InterPro; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR Pfam; PF00227; Proteasome; 1. DR PRINTS; PR00141; PROTEASOME. DR SUPFAM; SSF56235; SSF56235; 1. DR PROSITE; PS00854; PROTEASOME_BETA_1; 1. DR PROSITE; PS51476; PROTEASOME_BETA_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001450}; KW Hydrolase {ECO:0000256|RuleBase:RU000694}; KW Nucleus {ECO:0000256|SAAS:SAAS00039288}; KW Protease {ECO:0000256|RuleBase:RU000694}; KW Proteasome {ECO:0000256|RuleBase:RU000694, KW ECO:0000313|EMBL:AAN35309.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001450}; KW Threonine protease {ECO:0000256|RuleBase:RU000694}. 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 //