ID   PSB5_DICDI              Reviewed;         272 AA.
AC   Q54BC8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Proteasome subunit beta type-5;
DE            EC=3.4.25.1;
DE   Flags: Precursor;
GN   Name=psmB5; ORFNames=DDB_G0293784;
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=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).
RN   [2]
RP   IDENTIFICATION IN THE PROTEASOME COMPLEX.
RX   PubMed=8130037; DOI=10.1006/jsbi.1993.1044;
RA   Schauer T.M., Nesper M., Kehl M., Lottspeich F., Mueller-Taubenberger A.,
RA   Gerisch G., Baumeister W.;
RT   "Proteasomes from Dictyostelium discoideum: characterization of structure
RT   and function.";
RL   J. Struct. Biol. 111:135-147(1993).
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. The proteasome has an ATP-dependent proteolytic activity (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1;
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. {ECO:0000269|PubMed:8130037}.
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}.
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DR   EMBL; AAFI02000219; EAL60569.1; -; Genomic_DNA.
DR   RefSeq; XP_628966.1; XM_628964.1.
DR   AlphaFoldDB; Q54BC8; -.
DR   SMR; Q54BC8; -.
DR   STRING; 44689.Q54BC8; -.
DR   MEROPS; T01.012; -.
DR   PaxDb; 44689-DDB0232959; -.
DR   EnsemblProtists; EAL60569; EAL60569; DDB_G0293784.
DR   GeneID; 8629394; -.
DR   KEGG; ddi:DDB_G0293784; -.
DR   dictyBase; DDB_G0293784; psmB5.
DR   eggNOG; KOG0175; Eukaryota.
DR   HOGENOM; CLU_035750_7_0_1; -.
DR   InParanoid; Q54BC8; -.
DR   OMA; NLGMAMQ; -.
DR   PhylomeDB; Q54BC8; -.
DR   Reactome; R-DDI-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-DDI-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-DDI-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-DDI-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DDI-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-DDI-5689603; UCH proteinases.
DR   Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR   Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR   Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-DDI-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-DDI-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-DDI-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-DDI-8951664; Neddylation.
DR   Reactome; R-DDI-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q54BC8; -.
DR   Proteomes; UP000002195; Chromosome 6.
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:0004175; F:endopeptidase activity; IDA:dictyBase.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IDA:dictyBase.
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; 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; PS51476; PROTEASOME_BETA_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW   Threonine protease; Zymogen.
FT   PROPEP          1..62
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000327484"
FT   CHAIN           63..272
FT                   /note="Proteasome subunit beta type-5"
FT                   /id="PRO_0000327485"
FT   ACT_SITE        63
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   272 AA;  30280 MW;  9C6D656C754404C4 CRC64;
     MINIDFDNIE QSQPTLYDTL ASDVKFLNTP HFELPPNANP GDFLRETFDH PSAPKALEFA
     HGTTTLAFVY GGGIIVSVDS KSTQGPYVAS RSVKKVIEIT PTLLGTMAGG AADCSFWERE
     LGRRCRLYEL RNKELISVAA ASKILANIVY SYKGYGLSMG TMITGWDKTG PQLYYVDNDG
     TRLHGQRFSC GSGSTYAYGV LDTGFKWDMN DEEAYELGRR AVYHATHRDA YSGGAINVYH
     VQKDGWKKIS SDDCFKLYQK YYNIVPINKP AN
//