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Database: UniProt
Entry: H0GTS4_SACCK
LinkDB: H0GTS4_SACCK
Original site: H0GTS4_SACCK 
ID   H0GTS4_SACCK            Unreviewed;       516 AA.
AC   H0GTS4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Rpn3p {ECO:0000313|EMBL:EHN02697.1};
GN   ORFNames=VIN7_6667 {ECO:0000313|EMBL:EHN02697.1};
OS   Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS   (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN02697.1, ECO:0000313|Proteomes:UP000009009};
RN   [1] {ECO:0000313|EMBL:EHN02697.1, ECO:0000313|Proteomes:UP000009009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VIN7 {ECO:0000313|EMBL:EHN02697.1,
RC   ECO:0000313|Proteomes:UP000009009};
RX   PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT   genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT   origins.";
RL   FEMS Yeast Res. 12:88-96(2012).
CC   -!- SIMILARITY: Belongs to the proteasome subunit S3 family.
CC       {ECO:0000256|ARBA:ARBA00007912}.
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:EHN02697.1}.
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DR   EMBL; AGVY01000192; EHN02697.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0GTS4; -.
DR   HOGENOM; CLU_019858_1_2_1; -.
DR   PhylomeDB; H0GTS4; -.
DR   Proteomes; UP000009009; Unassembled WGS sequence.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:UniProt.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   InterPro; IPR013586; 26S_Psome_reg_C.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10758:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3; 1.
DR   PANTHER; PTHR10758; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 3/COP9 SIGNALOSOME COMPLEX SUBUNIT 3; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF08375; Rpn3_C; 1.
DR   SMART; SM00753; PAM; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
FT   DOMAIN          263..443
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          478..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  59787 MW;  D359C7CB8C642330 CRC64;
     MDVDSSGAND LHHSERKYAE QDQIQELLNV LNEISKTTIT LDPRYIWRSL KDLSSLRNQE
     LLNAETLSFT VNVLYPDSSS FKKNLLKFIN SNHKSSVSDS DELRNSYPAS FYSVNTEQKT
     IEVTPEINCF IHLLVQLFLW DSKQLQELVR FNRKVVIPKL LCFYNLRSLN LINAKLWFYI
     YLSHETLLRS SAENDDDNQN IILRSTMMKF LKIASLKHDN ETKAMLINLI LRDFLNNGEV
     DSASDFISKL EFPHIDVSST LEARYFFYLS KINAIQLDYS TANEYIIAAI RKAPHNCKSL
     GFLQQSNKLH CCIQLLMGDI PELSFFHQSN MQKSLLPYYH LTKTVKLGDL KKFTSTITKY
     KQLLLKDDTY QLCVRLRSNV IKTGIRIISL TYKKISLRDI CLKLNLDSEQ TVEYMVSRAI
     RDGVIEAKIN HEDGFIETTE LLNIYDSEDP QQVFDERIKF ANQLHDEYLV SMRYPEDKKT
     QQNEGNENGG NDDDILDGDL MDDMSDISDL DDLGFL
//
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