ID A0A1G4M795_LACFM Unreviewed; 215 AA.
AC A0A1G4M795;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=proteasome endopeptidase complex {ECO:0000256|ARBA:ARBA00012039};
DE EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039};
GN ORFNames=LAFE_0A06062G {ECO:0000313|EMBL:SCV99568.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCV99568.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|EMBL:SCV99568.1, ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6772 {ECO:0000313|EMBL:SCV99568.1};
RA Devillers H.;
RL Submitted (MAR-2016) 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; LT598487; SCV99568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4M795; -.
DR STRING; 4955.A0A1G4M795; -.
DR OMA; TFIYGYC; -.
DR OrthoDB; 754468at2759; -.
DR Proteomes; UP000190831; Chromosome a.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; cd03762; proteasome_beta_type_6; 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; 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:SF8; PROTEASOME SUBUNIT BETA; 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:UP000190831}.
FT ACT_SITE 20
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 215 AA; 23565 MW; FC43730C44693716 CRC64;
MNGIQVDVNH LKKGEVSLGT SIMAVTFKDG VILGADSRTT TGAYIANRVT DKLTRVHEKI
WCCRSGSAAD TQAVADIVQY YLDLYTSQFG EPSTKTAASV FKSLCYENKD NLTAGIIVAG
YDEKNKGEVY SIPLGGSVHK QPYAIAGSGS TFIYGYCDKN FKENMSKEET IDFMKNSLSQ
AIKWDGSSGG VIRMVVLTKD GAERLIFYPE EYENL
//
