ID   PSB6_YEAST     STANDARD;      PRT;   215 AA.
AC   P38624;
DT   01-OCT-1994 (Rel. 30, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   28-FEB-2003 (Rel. 41, Last annotation update)
DE   Proteasome component PRE3 precursor (EC 3.4.25.1) (Macropain subunit
DE   PRE3) (Proteinase YSCE subunit PRE3) (Multicatalytic endopeptidase
DE   complex subunit PRE3).
GN   PRE3 OR YJL001W OR J1407.
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=S288c;
RX   MEDLINE=94185793; PubMed=7907993;
RA   Enenkel C., Lehmann H., Kipper J., Gueckel R., Hilt W., Wolf D.H.;
RT   "PRE3, highly homologous to the human major histocompatibility
RT   complex-linked LMP2 (RING12) gene, codes for a yeast proteasome
RT   subunit necessary for the peptidylglutamyl-peptide hydrolyzing
RT   activity.";
RL   FEBS Lett. 341:193-196(1994).
RN   [2]
RP   REVISIONS TO N-TERMINUS.
RX   MEDLINE=95300795; PubMed=7781614;
RA   Chen P., Hochstrasser M.;
RT   "Biogenesis, structure and function of the yeast 20S proteasome.";
RL   EMBO J. 14:2620-2630(1995).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=S288c / FY1679;
RA   de Haan M., Smits P.H.M., Grivell L.A.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-215.
RX   MEDLINE=97242404; PubMed=9087403;
RA   Groll M., Ditzel L., Lowe J., Stock D., Bochtler M., Bartunik H.D.,
RA   Huber R.;
RT   "Structure of 20S proteasome from yeast at 2.4-A resolution.";
RL   Nature 386:463-471(1997).
CC   -!- FUNCTION: THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX
CC       WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG,
CC       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. PRE3 AND PRE4 ARE NECESSARY FOR THE PEPTIDYL-GLUTAMYL-
CC       PEPTIDE-HYDROLYZING ACTIVITY.
CC   -!- FUNCTION: THIS SUBUNIT IS NECESSARY FOR THE PEPTIDYLGLUTAMYL-
CC       PEPTIDE HYDROLYZING ACTIVITY.
CC   -!- CATALYTIC ACTIVITY: Cleavage at peptide bonds with very broad
CC       specificity.
CC   -!- PATHWAY: Involved in an ATP/ubiquitin-dependent non-lysosomal
CC       proteolytic pathway.
CC   -!- SUBUNIT: The yeast proteasome seems to be composed of 14 different
CC       subunits which form a highly ordered ring-shaped structure.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic and nuclear.
CC   -!- SIMILARITY: Belongs to peptidase family T1B.
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DR   EMBL; X78991; CAA55591.1; ALT_INIT.
DR   EMBL; Z49276; CAA89290.1; -.
DR   EMBL; Z49277; CAA89292.1; -.
DR   EMBL; X87611; CAA60921.1; ALT_INIT.
DR   EMBL; X86020; CAA60015.1; -.
DR   EMBL; S78566; AAB34629.1; -.
DR   PIR; S61337; S61337.
DR   PDB; 1RYP; 15-APR-98.
DR   MEROPS; T01.010; -.
DR   SGD; S0003538; PRE3.
DR   InterPro; IPR000243; Proteasome_B.
DR   InterPro; IPR001353; Protsme_protease.
DR   Pfam; PF00227; proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
DR   PROSITE; PS00854; PROTEASOME_B; 1.
KW   Proteasome; Hydrolase; Protease; 3D-structure; Zymogen.
FT   PROPEP        1     19       BY SIMILARITY.
FT   CHAIN        20    215       PROTEASOME COMPONENT PRE3.
SQ   SEQUENCE   215 AA;  23547 MW;  BD1FCE649678D86B CRC64;
     MNGIQVDINR LKKGEVSLGT SIMAVTFKDG VILGADSRTT TGAYIANRVT DKLTRVHDKI
     WCCRSGSAAD TQAIADIVQY HLELYTSQYG TPSTETAASV FKELCYENKD NLTAGIIVAG
     YDDKNKGEVY TIPLGGSVHK LPYAIAGSGS TFIYGYCDKN FRENMSKEET VDFIKHSLSQ
     AIKWDGSSGG VIRMVVLTAA GVERLIFYPD EYEQL
//