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Database: UniProt
Entry: G0VJ79_NAUCC
LinkDB: G0VJ79_NAUCC
Original site: G0VJ79_NAUCC 
ID   G0VJ79_NAUCC            Unreviewed;       264 AA.
AC   G0VJ79;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=proteasome endopeptidase complex {ECO:0000256|ARBA:ARBA00012039};
DE            EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039};
GN   Name=NCAS0H02480 {ECO:0000313|EMBL:CCC71558.1};
GN   OrderedLocusNames=NCAS_0H02480 {ECO:0000313|EMBL:CCC71558.1};
OS   Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS   1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC71558.1, ECO:0000313|Proteomes:UP000001640};
RN   [1] {ECO:0000313|EMBL:CCC71558.1, ECO:0000313|Proteomes:UP000001640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC   {ECO:0000313|Proteomes:UP000001640};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain:CBS 4309;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Naumovozyma castellii.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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: 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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; HE576759; CCC71558.1; -; Genomic_DNA.
DR   RefSeq; XP_003677905.1; XM_003677857.1.
DR   AlphaFoldDB; G0VJ79; -.
DR   STRING; 1064592.G0VJ79; -.
DR   MEROPS; T01.011; -.
DR   GeneID; 11525275; -.
DR   KEGG; ncs:NCAS_0H02480; -.
DR   eggNOG; KOG0173; Eukaryota.
DR   HOGENOM; CLU_035750_3_0_1; -.
DR   InParanoid; G0VJ79; -.
DR   OMA; VDKTGPH; -.
DR   OrthoDB; 5485745at2759; -.
DR   Proteomes; UP000001640; Chromosome 8.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IEA:UniProt.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR   CDD; cd03763; proteasome_beta_type_7; 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; IPR024689; Proteasome_bsu_C.
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:SF4; PROTEASOME SUBUNIT BETA TYPE-7; 1.
DR   Pfam; PF12465; Pr_beta_C; 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   4: Predicted;
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001640}.
FT   DOMAIN          223..258
FT                   /note="Proteasome beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12465"
FT   ACT_SITE        31
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ   SEQUENCE   264 AA;  28180 MW;  58F2C145F9DEBCE4 CRC64;
     MAGLSFDNYQ RNAALAAKSH SQQPKATSTG TTIVGVKYAN GVIIAADTRS TQGPIVANKN
     CAKLHRISPR IWCAGAGTAA DTEAVTQLIG SNIELHSLYT SREPRVVSAL QMLKQHLFKY
     QGHIGAYLIV AGTDPTGAHL FSIHAHGSTD VGYYLSLGSG SLAAMAVLES HWEPEMSKEA
     AVELASQAIQ AGIFNDLGSG SNVDVCVMEV GKDAEYLRNY LTPNVREAKQ NSYKFARGTT
     AVLRESIINV CEIDEEEVCV HAAA
//
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