ID Q8IJT1_PLAF7 Unreviewed; 271 AA. AC Q8IJT1; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 150. DE RecName: Full=Proteasome subunit beta {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., RA Eisen J.A., Rutherford K., 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., 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.; RT "Genome sequence of the human malaria parasite Plasmodium falciparum."; RL Nature 419:498-511(2002). RN [2] {ECO:0007829|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:0007829|PDB:6MUV, ECO:0007829|PDB:6MUW} 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. 4:1990-2000(2019). RN [4] {ECO:0007829|PDB:7LXT, ECO:0007829|PDB:7LXU} RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 61-271. RX PubMed=34548400; DOI=10.1073/pnas.2107213118; RA Xie S.C., Metcalfe R.D., Mizutani H., Puhalovich T., Hanssen E., RA Morton C.J., Du Y., Dogovski C., Huang S.C., Ciavarri J., Hales P., RA Griffin R.J., Cohen L.H., Chuang B.C., Wittlin S., Deni I., Yeo T., RA Ward K.E., Barry D.C., Liu B., Gillett D.L., Crespo-Fernandez B.F., RA Ottilie S., Mittal N., Churchyard A., Ferguson D., Aguiar A.C.C., RA Guido R.V.C., Baum J., Hanson K.K., Winzeler E.A., Gamo F.J., Fidock D.A., RA Baud D., Parker M.W., Brand S., Dick L.R., Griffin M.D.W., Gould A.E., RA Tilley L.; RT "Design of proteasome inhibitors with oral efficacy in vivo against RT Plasmodium falciparum and selectivity over the human proteasome."; RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021). CC -!- FUNCTION: Component of the proteasome, a multicatalytic proteinase CC complex which is characterized by its ability to cleave peptides with CC Arg, 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: CC Reaction=Cleavage of peptide bonds with very broad specificity.; CC EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198}; CC -!- SUBUNIT: Component of the proteasome complex. CC {ECO:0000256|RuleBase:RU004203}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}. CC Nucleus {ECO:0000256|RuleBase:RU004203}. 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 PDB; 7LXT; EM; 3.40 A; L/Z=61-271. DR PDB; 7LXU; EM; 3.10 A; L/Z=61-271. DR PDBsum; 5FMG; -. DR PDBsum; 6MUV; -. DR PDBsum; 6MUW; -. DR PDBsum; 6MUX; -. DR AlphaFoldDB; Q8IJT1; -. DR EMDB; EMD-23574; -. DR EMDB; EMD-23575; -. DR EMDB; EMD-9257; -. DR EMDB; EMD-9258; -. DR EMDB; EMD-9259; -. DR SMR; Q8IJT1; -. DR DIP; DIP-43048N; -. DR IntAct; Q8IJT1; 14. DR STRING; 36329.Q8IJT1; -. DR GuidetoPHARMACOLOGY; 3088; -. DR MEROPS; T01.A15; -. DR PaxDb; 5833-PF10_0111; -. DR EnsemblProtists; CZT98364; CZT98364; PF3D7_1011400. DR GeneID; 810269; -. DR KEGG; pfa:PF3D7_1011400; -. DR VEuPathDB; PlasmoDB:PF3D7_1011400; -. DR HOGENOM; CLU_035750_7_3_1; -. DR InParanoid; Q8IJT1; -. DR OMA; NLGMAMQ; -. DR OrthoDB; 4492251at2759; -. DR PhylomeDB; Q8IJT1; -. DR Reactome; R-PFA-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-PFA-174113; SCF-beta-TrCP mediated degradation of Emi1. 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-8951664; Neddylation. DR Reactome; R-PFA-9755511; KEAP1-NFE2L2 pathway. 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:0019774; C:proteasome core complex, beta-subunit complex; IBA:GO_Central. DR GO; GO:0004175; F:endopeptidase activity; ISS:GeneDB. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:GeneDB. DR CDD; cd03761; proteasome_beta_type_5; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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 PANTHER; PTHR32194:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1. DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1. DR Pfam; PF00227; Proteasome; 1. DR PRINTS; PR00141; PROTEASOME. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 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:0007829|PDB:5FMG, ECO:0007829|PDB:6MUV}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU004203}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CZT98364.1}; KW Nucleus {ECO:0000256|RuleBase:RU004203}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203}; KW Reference proteome {ECO:0000313|Proteomes:UP000001450}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT ACT_SITE 61 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1" FT DISULFID 112..157 FT /evidence="ECO:0007829|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 //