ID   PSB2_ENCCU              Reviewed;         227 AA.
AC   Q8SQN7;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Probable proteasome subunit beta type-2;
DE            EC=3.4.25.1;
DE   AltName: Full=26S proteasome beta-type subunit PUP1;
DE   AltName: Full=Multicatalytic endopeptidase complex subunit PUP1;
DE   Flags: Precursor;
GN   Name=PUP1; OrderedLocusNames=ECU09_0720;
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   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: The proteasome degrades poly-ubiquitinated proteins in the
CC       cytoplasm and in the nucleus. It is essential for the regulated
CC       turnover of proteins and for the removal of misfolded proteins. The
CC       proteasome is a multicatalytic proteinase complex that is characterized
CC       by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu
CC       adjacent to the leaving group at neutral or slightly basic pH. It has
CC       an ATP-dependent proteolytic activity (By 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 (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}.
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DR   EMBL; AL590451; CAD27045.1; -; Genomic_DNA.
DR   RefSeq; XP_955626.1; XM_950533.1.
DR   AlphaFoldDB; Q8SQN7; -.
DR   SMR; Q8SQN7; -.
DR   STRING; 284813.Q8SQN7; -.
DR   MEROPS; T01.011; -.
DR   VEuPathDB; MicrosporidiaDB:ECU09_0720; -.
DR   HOGENOM; CLU_035750_3_0_1; -.
DR   InParanoid; Q8SQN7; -.
DR   OMA; GRYHFAP; -.
DR   OrthoDB; 5485745at2759; -.
DR   Proteomes; UP000000819; Chromosome IX.
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:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR   CDD; cd03763; proteasome_beta_type_7; 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:SF4; PROTEASOME SUBUNIT BETA TYPE-7; 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   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW   Threonine protease.
FT   PROPEP          1..6
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000391409"
FT   CHAIN           7..227
FT                   /note="Probable proteasome subunit beta type-2"
FT                   /id="PRO_0000382761"
FT   ACT_SITE        7
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   227 AA;  24766 MW;  D7069F03AB8BAF53 CRC64;
     MITKTGTTIV GMKYKTGVIL AADTRSTQGP VVSDKNCVKI HQITDKIMCC GAGTAADASR
     VARMASRELR LFQNKYLRLP LVSHFRKVCT QHLHKYGGGI GAALIVGGID SEGCHLYEIH
     PHGSENSALF VSLGSGSLGA IATLESRYRA MDKDEAIDLA CDAVKAGILN DLYSGSNIDV
     CVIDYSGVEF LRNYRRIGVS ENTDTLVYPL DSVRIKREEV FDIVEEY
//