ID I6NDR5_ERECY Unreviewed; 258 AA.
AC I6NDR5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=proteasome endopeptidase complex {ECO:0000256|ARBA:ARBA00012039};
DE EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039};
GN OrderedLocusNames=Ecym_5458 {ECO:0000313|EMBL:AET40207.1};
OS Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS NRRL Y-17582) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=931890 {ECO:0000313|EMBL:AET40207.1, ECO:0000313|Proteomes:UP000006790};
RN [1] {ECO:0000313|EMBL:AET40207.1, ECO:0000313|Proteomes:UP000006790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC {ECO:0000313|Proteomes:UP000006790};
RX PubMed=22384365;
RA Wendland J., Walther A.;
RT "Genome evolution in the Eremothecium clade of the Saccharomyces complex
RT revealed by comparative genomics.";
RL G3 (Bethesda) 1:539-548(2011).
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; CP002501; AET40207.1; -; Genomic_DNA.
DR RefSeq; XP_003647024.1; XM_003646976.1.
DR AlphaFoldDB; I6NDR5; -.
DR STRING; 931890.I6NDR5; -.
DR MEROPS; T01.011; -.
DR GeneID; 11472033; -.
DR KEGG; erc:Ecym_5458; -.
DR eggNOG; KOG0173; Eukaryota.
DR HOGENOM; CLU_035750_3_0_1; -.
DR InParanoid; I6NDR5; -.
DR OMA; KQHLFRH; -.
DR OrthoDB; 5485745at2759; -.
DR Proteomes; UP000006790; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:UP000006790}.
FT DOMAIN 222..249
FT /note="Proteasome beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12465"
FT ACT_SITE 30
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 258 AA; 27808 MW; 1E81E3741F33122D CRC64;
MAGLSFDNYQ RNQYLTAQSH KQPQATSTGT TIVGVKFENG VVIAADTRST QGPIVANKNC
EKLHKISSRI WCAGAGTAAD TDAVTGLIGS NLELHSLFTG REPRVVSALQ KLKQHLFKYQ
GHIGAYLIVA GVDPTGAHLF SVHAHGSTDV GYYQSLGSGS LAAMAVLEAN WKEHLTKEEA
IKLAADAIEA GIWNDLGSGS NVDVCVMEVG KDAELLRNYI TPNVREAKQK SYKFDRGTTA
VLKESILEVY DEEIVTLS
//
