ID   PSB4_CRYNJ              Reviewed;         224 AA.
AC   P0CQ12; Q00826; Q55WC0; Q5KJX9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Probable proteasome subunit beta type-4;
GN   Name=CPR1; OrderedLocusNames=CNC04990;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8675296; DOI=10.1128/iai.64.6.1977-1983.1996;
RA   Chang Y.C., Penoyer L.A., Kwon-Chung K.J.;
RT   "The second capsule gene of Cryptococcus neoformans, CAP64, is essential
RT   for virulence.";
RL   Infect. Immun. 64:1977-1983(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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}.
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DR   EMBL; L40028; AAB06582.1; -; Genomic_DNA.
DR   EMBL; AE017343; AAW42482.1; -; Genomic_DNA.
DR   RefSeq; XP_569789.1; XM_569789.1.
DR   AlphaFoldDB; P0CQ12; -.
DR   SMR; P0CQ12; -.
DR   STRING; 214684.P0CQ12; -.
DR   PaxDb; 214684-P0CQ12; -.
DR   EnsemblFungi; AAW42482; AAW42482; CNC04990.
DR   GeneID; 3256830; -.
DR   KEGG; cne:CNC04990; -.
DR   VEuPathDB; FungiDB:CNC04990; -.
DR   eggNOG; KOG0177; Eukaryota.
DR   HOGENOM; CLU_035750_12_1_1; -.
DR   InParanoid; P0CQ12; -.
DR   OMA; RGPTVLK; -.
DR   OrthoDB; 158209at2759; -.
DR   Proteomes; UP000002149; Chromosome 3.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IBA:GO_Central.
DR   GO; GO:0061133; F:endopeptidase activator activity; IEA:EnsemblFungi.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   CDD; cd03758; proteasome_beta_type_2; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR035206; Proteasome_beta2.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR   PANTHER; PTHR11599:SF6; PROTEASOME SUBUNIT BETA TYPE-2; 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..224
FT                   /note="Probable proteasome subunit beta type-4"
FT                   /id="PRO_0000148052"
SQ   SEQUENCE   224 AA;  25239 MW;  A8EEF03E76170886 CRC64;
     MECSFGITGK DYVILASDMG AGRSIVRMKS DENKLKTLGP HLAMAFSGEP GDTNNFAEYI
     ERNMRLYNIR NHFPLLPPAA SAWVRRTLAE AIRSRHPYAV NLLLGGFDTT TSKPHLYWID
     YLGTKAIVPY AAHGMGVYVS LSTMDKWWYE DMDKKEGVDL LRKCIDETEK RLTIKFDFNC
     ILIDKNGIHK VDLSQADPIA NIQEHPQETE VEAPHPPIEV GISA
//