ID   PSB7_ENCCU              Reviewed;         226 AA.
AC   Q8SS01;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable proteasome subunit beta type-7;
DE   AltName: Full=26S proteasome beta-type subunit PRE4;
DE   AltName: Full=Multicatalytic endopeptidase complex subunit PRE4;
GN   Name=PRE4; OrderedLocusNames=ECU05_0290;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Non-catalytic component of the proteasome which degrades
CC       poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is
CC       essential for the regulated turnover of proteins and for the removal of
CC       misfolded proteins. The proteasome is a multicatalytic proteinase
CC       complex that 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. It has an ATP-dependent proteolytic activity (By
CC       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   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
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; AL590445; CAD26546.2; -; Genomic_DNA.
DR   RefSeq; NP_597369.1; NM_001041235.1.
DR   AlphaFoldDB; Q8SS01; -.
DR   SMR; Q8SS01; -.
DR   STRING; 284813.Q8SS01; -.
DR   GeneID; 859033; -.
DR   KEGG; ecu:ECU05_0290; -.
DR   VEuPathDB; MicrosporidiaDB:ECU05_0290; -.
DR   HOGENOM; CLU_072435_1_0_1; -.
DR   InParanoid; Q8SS01; -.
DR   OrthoDB; 1228942at2759; -.
DR   Proteomes; UP000000819; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR016295; Proteasome_beta4.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF5; PTHR11599:SF5; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PIRSF; PIRSF001213; Psome_endopept_beta; 1.
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   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..226
FT                   /note="Probable proteasome subunit beta type-7"
FT                   /id="PRO_0000382759"
SQ   SEQUENCE   226 AA;  25437 MW;  5C12A26F6871D17B CRC64;
     MRDFVTGTTV VSFRYRDGII MGADTRGSYG RLAKLSGVQR IFKVGDQTLL GMSGEISDMQ
     YLVKTLTILT QEDNRRIDPK GYHKMIQRIL YSARSKISPL NLSVCVGGLN AASDGDRRTH
     TREKMLGCVN HLGNFYFSDV VCTGIGGYLV LPFLRNRVEG REEEIAREEA IGLVEEAMRI
     LCYRDCNASN EIQVGYVDDQ GVHISDPYQI KTNWDVGLRE DEIVIE