ID Q8IJT1_PLAF7 Unreviewed; 271 AA. AC Q8IJT1; DT 01-MAR-2003, integrated into UniProtKB/TrEMBL. DT 01-MAR-2003, sequence version 1. DT 08-JUN-2016, entry version 101. 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}, PF3D7_1011400 GN {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: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=3D7 {ECO:0000313|EMBL:AAN35309.1}, and Isolate 3D7 RC {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., RA James K.D., Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., RA Kyes S., Chan M.-S., Nene V., Shallom S.J., Suh B., Peterson J., RA Angiuoli S., Pertea M., Allen J., Selengut J., Haft D., Mather M.W., RA Vaidya A.B., Martin D.M.A., Fairlamb A.H., Fraunholz M.J., Roos D.S., RA Ralph S.A., McFadden G.I., Cummings L.M., Subramanian G.M., RA Mungall C., Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., RA Davis R.W., Fraser C.M., Barrell B.G.; RT "Genome sequence of the human malaria parasite Plasmodium RT falciparum."; RL Nature 419:498-511(2002). RN [2] {ECO:0000313|EMBL:CZT98364.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=3D7 {ECO:0000313|EMBL:CZT98364.1}; RG P. falciparum Genome Sequencing Consortium; RA Aslett M., Brunk B., Gardner M., Berriman M.; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [3] {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. 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 Nucleus {ECO:0000256|RuleBase:RU000694}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00551005}. 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 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 ProteinModelPortal; Q8IJT1; -. DR SMR; Q8IJT1; 61-261. DR IntAct; Q8IJT1; 13. DR MINT; MINT-1554977; -. DR MEROPS; T01.A15; -. DR EnsemblProtists; PF10_0111:mRNA; PF10_0111:pep; PF10_0111. DR GeneDB; PF3D7_1011400.1:pep; -. DR GeneID; 810269; -. DR KEGG; pfa:PF10_0111; -. DR EuPathDB; PlasmoDB:PF3D7_1011400; -. DR HOGENOM; HOG000091082; -. DR InParanoid; Q8IJT1; -. DR KO; K02737; -. DR OMA; YEPATPN; -. DR PhylomeDB; Q8IJT1; -. DR Reactome; R-PFA-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-PFA-68949; Orc1 removal from chromatin. 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: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 Hydrolase {ECO:0000256|RuleBase:RU000694, KW ECO:0000313|EMBL:CZT98364.1}; KW Nucleus {ECO:0000256|SAAS:SAAS00435711}; 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}. 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 //