ID Q2HED6_CHAGB Unreviewed; 272 AA.
AC Q2HED6;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=proteasome endopeptidase complex {ECO:0000256|ARBA:ARBA00012039};
DE EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039};
GN ORFNames=CHGG_01418 {ECO:0000313|EMBL:EAQ93183.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ93183.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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}.
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DR EMBL; CH408029; EAQ93183.1; -; Genomic_DNA.
DR RefSeq; XP_001220639.1; XM_001220638.1.
DR AlphaFoldDB; Q2HED6; -.
DR STRING; 306901.Q2HED6; -.
DR MEROPS; T01.011; -.
DR GeneID; 4387449; -.
DR VEuPathDB; FungiDB:CHGG_01418; -.
DR eggNOG; KOG0173; Eukaryota.
DR HOGENOM; CLU_035750_3_0_1; -.
DR InParanoid; Q2HED6; -.
DR OMA; VDKTGPH; -.
DR OrthoDB; 5485745at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
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; 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; PS51476; PROTEASOME_BETA_2; 1.
PE 4: Predicted;
KW Proteasome {ECO:0000313|EMBL:EAQ93183.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT DOMAIN 221..254
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 272 AA; 29190 MW; 8E7399B8ED481C6E CRC64;
MPGFDFSNYN RNAALHARGV PLPKATSTGT TIVGCIYDGG VVIAADTRAT SGPIVADKNC
EKLHYIAPNI WCAGAGTAAD TEFTTALISS QLELHSLSTG RKARVVTCMT MLKQHLFRYQ
GHIGAYLVVA GVDPTGTHLF TVHAHGSTDK LPYVTMGSGS LAAMSVFETQ WKASLTQDEA
VKLCADAIEA GIWNDLGSGS NVDVAIITGE KTTLRRNYIK PNERTQKLKS YAFPKGTTAV
LNEKIIHKAD LSKFVSVHEL TEEGGDKMEV DT
//