ID Q8IJT1_PLAF7 Unreviewed; 271 AA. AC Q8IJT1; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 13-FEB-2019, entry version 125. DE RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203}; DE EC=3.4.25.1 {ECO:0000256|RuleBase:RU004203}; GN ORFNames=PF3D7_1011400 {ECO:0000313|EMBL:CZT98364.1}; OS Plasmodium falciparum (isolate 3D7). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=36329 {ECO:0000313|EMBL:CZT98364.1, ECO:0000313|Proteomes:UP000001450}; RN [1] {ECO:0000313|EMBL:CZT98364.1, 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., 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). RN [2] {ECO:0000213|PDB:5FMG} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 61-271, AND RP DISULFIDE BONDS. RX PubMed=26863983; DOI=10.1038/NATURE16936; RA Li H., O'Donoghue A.J., van der Linden W.A., Xie S.C., Yoo E., RA Foe I.T., Tilley L., Craik C.S., da Fonseca P.C., Bogyo M.; RT "Structure- and function-based design of Plasmodium-selective RT proteasome inhibitors."; RL Nature 530:233-236(2016). 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. {ECO:0000256|RuleBase:RU004203}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleavage of peptide bonds with very broad specificity.; CC EC=3.4.25.1; Evidence={ECO:0000256|RuleBase:RU004203}; CC -!- SUBUNIT: The 20S proteasome core is composed of 28 subunits that CC are arranged in four stacked rings, resulting in a barrel-shaped CC structure. The two end rings are each formed by seven alpha CC subunits, and the two central rings are each formed by seven beta CC subunits. {ECO:0000256|RuleBase:RU004203}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}. CC Nucleus {ECO:0000256|RuleBase:RU004203, CC ECO:0000256|SAAS:SAAS00551005}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. CC {ECO:0000256|RuleBase:RU004203}. 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; LN999944; CZT98364.1; -; Genomic_DNA. DR RefSeq; XP_001347396.1; XM_001347360.1. DR PDB; 5FMG; EM; 3.60 A; L/Z=61-271. DR PDBsum; 5FMG; -. DR SMR; Q8IJT1; -. DR DIP; DIP-43048N; -. DR IntAct; Q8IJT1; 14. DR MEROPS; T01.A15; -. DR PRIDE; Q8IJT1; -. DR EnsemblProtists; CZT98364; CZT98364; PF3D7_1011400. DR GeneDB; PF3D7_1011400.1:pep; -. DR GeneID; 810269; -. DR KEGG; pfa:PF3D7_1011400; -. DR EuPathDB; PlasmoDB:PF3D7_1011400; -. DR KO; K02737; -. DR OMA; NLGMAMQ; -. DR BioCyc; PLASMO:PF10_0111-MONOMER; -. DR Reactome; R-PFA-5689603; UCH proteinases. DR Reactome; R-PFA-5689880; Ub-specific processing proteases. DR Reactome; R-PFA-68949; Orc1 removal from chromatin. DR Proteomes; UP000001450; Chromosome 10. DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB. DR GO; GO:0005634; C:nucleus; IDA:GeneDB. DR GO; GO:0005839; C:proteasome core complex; ISS:GeneDB. DR GO; GO:0004175; F:endopeptidase activity; ISS:GeneDB. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central. DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:GeneDB. 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 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:5FMG}; KW Complete proteome {ECO:0000313|Proteomes:UP000001450}; KW Cytoplasm {ECO:0000256|RuleBase:RU004203}; KW Hydrolase {ECO:0000256|RuleBase:RU004203, KW ECO:0000313|EMBL:CZT98364.1}; KW Nucleus {ECO:0000256|RuleBase:RU004203, KW ECO:0000256|SAAS:SAAS00039288}; KW Protease {ECO:0000256|RuleBase:RU004203}; KW Proteasome {ECO:0000256|RuleBase:RU004203, KW ECO:0000313|EMBL:CZT98364.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001450}; KW Threonine protease {ECO:0000256|RuleBase:RU004203}. FT DISULFID 112 157 {ECO:0000213|PDB:5FMG}. 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 //