ID Q8IJT1_PLAF7 Unreviewed; 271 AA. AC Q8IJT1; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 22-APR-2020, entry version 131. 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; Sar; 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.D., RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S., RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M., RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A., RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I., RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J., RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.; RT "Genome sequence of the human malaria parasite Plasmodium 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 DISULFIDE RP 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., Foe I.T., RA Tilley L., Craik C.S., da Fonseca P.C., Bogyo M.; RT "Structure- and function-based design of Plasmodium-selective proteasome RT inhibitors."; RL Nature 530:233-236(2016). RN [3] {ECO:0000213|PDB:6MUV, ECO:0000213|PDB:6MUW, ECO:0000213|PDB:6MUX} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 61-271. RX PubMed=31384003; DOI=10.1038/s41564-019-0524-4; RA Xie S.C., Metcalfe R.D., Hanssen E., Yang T., Gillett D.L., Leis A.P., RA Morton C.J., Kuiper M.J., Parker M.W., Spillman N.J., Wong W., Tsu C., RA Dick L.R., Griffin M.D.W., Tilley L.; RT "The structure of the PA28-20S proteasome complex from Plasmodium RT falciparum and implications for proteostasis."; RL Nat. Microbiol. 0:0-0(2019). CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr, CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic CC 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 are CC arranged in four stacked rings, resulting in a barrel-shaped structure. CC The two end rings are each formed by seven alpha subunits, and the two CC central rings are each formed by seven beta subunits. CC {ECO:0000256|RuleBase:RU004203}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}. CC Nucleus {ECO:0000256|RuleBase:RU004203, 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 PDB; 6MUV; EM; 3.80 A; L/Z=61-271. DR PDB; 6MUW; EM; 3.60 A; L/Z=61-271. DR PDB; 6MUX; EM; 3.90 A; L/Z=61-271. DR PDBsum; 5FMG; -. DR PDBsum; 6MUV; -. DR PDBsum; 6MUW; -. DR PDBsum; 6MUX; -. 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 HOGENOM; CLU_035750_7_3_1; -. DR KO; K02737; -. DR OMA; NLGMAMQ; -. DR BioCyc; PLASMO:PF10_0111-MONOMER; -. DR Reactome; R-PFA-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-PFA-382556; ABC-family proteins mediated transport. DR Reactome; R-PFA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-PFA-5687128; MAPK6/MAPK4 signaling. 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 Reactome; R-PFA-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-PFA-983168; Antigen processing: Ubiquitination & Proteasome degradation. 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, ECO:0000213|PDB:6MUV, KW ECO:0000213|PDB:6MUW, ECO:0000213|PDB:6MUX}; KW Cytoplasm {ECO:0000256|RuleBase:RU004203}; KW Hydrolase {ECO:0000256|RuleBase:RU004203, ECO:0000313|EMBL:CZT98364.1}; KW Nucleus {ECO:0000256|RuleBase:RU004203, ECO:0000256|SAAS:SAAS00435711}; KW Protease {ECO:0000256|RuleBase:RU004203}; KW Proteasome {ECO:0000256|RuleBase:RU004203, ECO:0000313|EMBL:CZT98364.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001450}; KW Threonine protease {ECO:0000256|RuleBase:RU004203}. FT ACT_SITE 61 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1" FT DISULFID 112..157 FT /evidence="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 //