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   29-MAR-2004 (Rel. 43, 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; 1G65; 21-NOV-01.
DR   PDB; 1RYP; 15-APR-98.
DR   GermOnline; 141617; -.
DR   MEROPS; T01.010; -.
DR   SGD; S0003538; PRE3.
DR   InterPro; IPR000243; Pept_T1A_subB.
DR   InterPro; IPR001353; Peptidase_T1.
DR   Pfam; PF00227; proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
DR   PROSITE; PS00854; PROTEASOME_B; 1.
KW   Proteasome; Hydrolase; Protease; 3D-structure; Zymogen;
KW   Threonine protease.
FT   PROPEP        1     19       By similarity.
FT   CHAIN        20    215       Proteasome component PRE3.
FT   TURN         13     14
FT   STRAND       17     17
FT   STRAND       22     27
FT   TURN         28     29
FT   STRAND       30     35
FT   STRAND       39     41
FT   TURN         42     43
FT   STRAND       44     47
FT   STRAND       53     57
FT   TURN         58     59
FT   STRAND       60     67
FT   HELIX        68     89
FT   HELIX        94    107
FT   TURN        108    111
FT   STRAND      114    122
FT   TURN        123    125
FT   STRAND      126    132
FT   TURN        134    135
FT   STRAND      139    141
FT   STRAND      143    146
FT   HELIX       148    153
FT   HELIX       154    160
FT   TURN        163    164
FT   HELIX       167    184
FT   STRAND      185    185
FT   TURN        186    187
FT   STRAND      192    198
FT   TURN        199    200
FT   STRAND      201    207
FT   HELIX       209    212
FT   TURN        213    213
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
//