ID PSB1_DICDI Reviewed; 236 AA. AC Q86A21; Q1ZXN1; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 24-JAN-2024, entry version 127. DE RecName: Full=Proteasome subunit beta type-1; GN Name=psmB1; ORFNames=DDB_G0272969; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=12097910; DOI=10.1038/nature00847; RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., RA Noegel A.A.; RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum."; RL Nature 418:79-85(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). CC -!- FUNCTION: Non-catalytic component of the proteasome, a multicatalytic CC proteinase complex which is characterized by its ability to cleave CC peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group CC at neutral or slightly basic pH. The proteasome has an ATP-dependent CC proteolytic activity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two CC 19S regulatory subunits. The 20S proteasome core is composed of 28 CC subunits that are arranged in four stacked rings, resulting in a CC barrel-shaped structure. The two end rings are each formed by seven CC alpha subunits, and the two central rings are each formed by seven beta CC subunits. The catalytic chamber with the active sites is on the inside CC of the barrel (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. CC Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE- CC ProRule:PRU00809}. 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; AAFI02000008; EAS66954.1; -; Genomic_DNA. DR RefSeq; XP_001134620.1; XM_001134620.1. DR AlphaFoldDB; Q86A21; -. DR SMR; Q86A21; -. DR BioGRID; 1243573; 1. DR STRING; 44689.Q86A21; -. DR MEROPS; T01.A14; -. DR PaxDb; 44689-DDB0232957; -. DR EnsemblProtists; EAS66954; EAS66954; DDB_G0272969. DR GeneID; 8618570; -. DR KEGG; ddi:DDB_G0272969; -. DR dictyBase; DDB_G0272969; psmB1. DR eggNOG; KOG0179; Eukaryota. DR HOGENOM; CLU_035750_1_1_1; -. DR InParanoid; Q86A21; -. DR OMA; MLYYKRF; -. DR PhylomeDB; Q86A21; -. DR PRO; PR:Q86A21; -. DR Proteomes; UP000002195; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IPI:dictyBase. DR GO; GO:0005634; C:nucleus; IPI:dictyBase. DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:dictyBase. DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:dictyBase. DR CDD; cd03757; proteasome_beta_type_1; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1. DR PANTHER; PTHR32194:SF2; PROTEASOME SUBUNIT BETA TYPE-1; 1. DR Pfam; PF00227; Proteasome; 1. 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 3: Inferred from homology; KW Cytoplasm; Nucleus; Proteasome; Reference proteome. FT CHAIN 1..236 FT /note="Proteasome subunit beta type-1" FT /id="PRO_0000328481" SQ SEQUENCE 236 AA; 26380 MW; F5BC59291CA38DE2 CRC64; METLKLSALP EKDKQQPISH GRFEAYVDNG GTVLAVAGKD YCVIAGDTRM SDGGYGIQTR KYTKIFQLTK KCVLATSGMQ ADTIALQKRL KSMLESFEKE HGKPMSTPAI AQFLSNTLYY KRFFPYYTFN LVAGVDEQGE GWIWTYDAVG SHERVKYSSQ GSGNQLVIPL LDNQVAKFNQ QIVEGNKDVS CEQVVSFVKD SITSAGERDI YTGDFADIVV VDKNGVHWEK FELKLD //