ID   PRCD_YEAST     STANDARD;      PRT;   215 AA.
AC   P38624;
DT   01-OCT-1994 (REL. 30, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   15-DEC-1998 (REL. 37, LAST ANNOTATION UPDATE)
DE   PROTEASOME COMPONENT PRE3 PRECURSOR (EC 3.4.99.46) (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; HEMIASCOMYCETES; SACCHAROMYCETALES;
OC   SACCHAROMYCETACEAE; SACCHAROMYCES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=S288C;
RX   MEDLINE; 94185793.
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-TERMINAL.
RX   MEDLINE; 95300795.
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 EMBL/GENBANK/DDBJ DATA BANKS.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 11-215.
RX   MEDLINE; 97242404.
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
CC       ARG, PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT
CC       NEUTRAL OR SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT
CC       PROTEOLYTIC ACTIVITY. PRE3 AND PRE4 ARE NECESSARY FOR THE
CC       PEPTIDYL-GLUTAMYL-PEPTIDE-HYDROLYZING ACTIVITY.
CC   -!- FUNCTION: THIS SUBUNIT IS NECESSARY FOR THE PEPTIDYLGLUTAMYL-
CC       PEPTIDE HYDROLYZING ACTIVITY.
CC   -!- PATHWAY: IS INVOLVED IN AN ATP/UBIQUITIN-DEPENDENT NON-LYSOSOMAL
CC       PROTEOLYTIC PATHWAY.
CC   -!- SUBUNIT: 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; ALSO KNOWN AS THE
CC       PROTEASOME B-TYPE FAMILY. BELONGS TO THE DELTA CHAIN SUBFAMILY.
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DR   EMBL; X78991; G476044; ALT_INIT.
DR   EMBL; Z49276; E318849; -.
DR   EMBL; Z49277; E318881; -.
DR   EMBL; X87611; G854572; ALT_INIT.
DR   EMBL; X86020; G780279; -.
DR   EMBL; S78566; G1041974; -.
DR   PIR; S43669; S43669.
DR   PDB; 1RYP; 15-APR-98.
DR   SGD; L0001485; PRE3.
DR   PROSITE; PS00854; PROTEASOME_B; 1.
DR   PFAM; PF00227; proteasome; 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;  CDCA9B66 CRC32;
     MNGIQVDINR LKKGEVSLGT SIMAVTFKDG VILGADSRTT TGAYIANRVT DKLTRVHDKI
     WCCRSGSAAD TQAIADIVQY HLELYTSQYG TPSTETAASV FKELCYENKD NLTAGIIVAG
     YDDKNKGEVY TIPLGGSVHK LPYAIAGSGS TFIYGYCDKN FRENMSKEET VDFIKHSLSQ
     AIKWDGSSGG VIRMVVLTAA GVERLIFYPD EYEQL
//