ID   A0A094EJL8_9PEZI        Unreviewed;       229 AA.
AC   A0A094EJL8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN   ORFNames=V499_03754 {ECO:0000313|EMBL:KFY76658.1};
OS   Pseudogymnoascus sp. VKM F-103.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY76658.1, ECO:0000313|Proteomes:UP000029295};
RN   [1] {ECO:0000313|EMBL:KFY76658.1, ECO:0000313|Proteomes:UP000029295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY76658.1,
RC   ECO:0000313|Proteomes:UP000029295};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the proteasome, a multicatalytic proteinase
CC       complex which 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. The proteasome has an ATP-dependent proteolytic
CC       activity. {ECO:0000256|RuleBase:RU004203}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198};
CC   -!- SUBUNIT: Component of the proteasome complex.
CC       {ECO:0000256|RuleBase:RU004203}.
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:0000256|ARBA:ARBA00026071}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}.
CC       Nucleus {ECO:0000256|RuleBase:RU004203}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family.
CC       {ECO:0000256|RuleBase:RU004203}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY76658.1}.
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DR   EMBL; JPKB01000569; KFY76658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094EJL8; -.
DR   HOGENOM; CLU_035750_5_2_1; -.
DR   Proteomes; UP000029295; Unassembled WGS sequence.
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; IEA:UniProt.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR   CDD; cd03762; proteasome_beta_type_6; 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; 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:SF8; PROTEASOME SUBUNIT BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
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 {ECO:0000256|RuleBase:RU004203};
KW   Nucleus {ECO:0000256|RuleBase:RU004203};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203}.
FT   ACT_SITE        30
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ   SEQUENCE   229 AA;  24636 MW;  891D777E895F43BD CRC64;
     MEFGNSGMLN EDGIHVDMDR LKKGEVNLGT SIMAINFKDG VILGADSRTT TGAYIANRVT
     DKLTQVHDTI WCCRSGSAAD TQAVADIVHY QLGMYGIQNG APPTTQVAAA MFQELCYNNK
     DRLSAGLIIA GWDERHGGQV YSIPLGGSLH KQSYAIGGSG STYIYGYCDA NWQEGFEEAE
     AVDFVKGALA EAIKWDGSSG GVIRMVVLTK KGAVRHLYLP DNGYKVNVA
//