ID D4DGJ4_TRIVH Unreviewed; 275 AA.
AC D4DGJ4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=proteasome endopeptidase complex {ECO:0000256|ARBA:ARBA00012039};
DE EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039};
GN ORFNames=TRV_06298 {ECO:0000313|EMBL:EFE39024.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE39024.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(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 -!- 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:EFE39024.1}.
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DR EMBL; ACYE01000359; EFE39024.1; -; Genomic_DNA.
DR RefSeq; XP_003019669.1; XM_003019623.1.
DR AlphaFoldDB; D4DGJ4; -.
DR MEROPS; T01.011; -.
DR GeneID; 9583586; -.
DR KEGG; tve:TRV_06298; -.
DR HOGENOM; CLU_035750_3_0_1; -.
DR OrthoDB; 5485745at2759; -.
DR Proteomes; UP000008383; 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;
FT DOMAIN 222..257
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 275 AA; 29749 MW; 75E1F00DD26AA6B8 CRC64;
MPGFDFSNYN RNRALHAKGV PLPKATSTGT TIVGCIFDGG VVIAADTRAT SGPIVADKNC
EKIHYIAPSI WCAGAGTAAD TEFTTNLISS NIELHSLSTG RAPRVATCMT MLKQHLFRYQ
GHIGAYLVVA GVDPTGTHLF TVHAHGSTDK LPYVTMGSGS LAAMSVFESM WKPSLTKDEA
IKLASEAIQA GIWNDLGSGS NVDVCVMEKD KPTKVMRNYL TPNERGEKER SYKFQRGTTA
WLDEQVITKA DLARYVTIEE LGGEEAVAER MDVDV
//
