ID A0A1Y2FN34_9BASI Unreviewed; 281 AA. AC A0A1Y2FN34; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 27-NOV-2024, entry version 22. DE RecName: Full=proteasome endopeptidase complex {ECO:0000256|ARBA:ARBA00012039}; DE EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039}; GN ORFNames=BCR35DRAFT_302804 {ECO:0000313|EMBL:ORY85339.1}; OS Leucosporidium creatinivorum. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; OC Microbotryomycetes; Leucosporidiales; Leucosporidium. OX NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY85339.1, ECO:0000313|Proteomes:UP000193467}; RN [1] {ECO:0000313|EMBL:ORY85339.1, ECO:0000313|Proteomes:UP000193467} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=62-1032 {ECO:0000313|EMBL:ORY85339.1, RC ECO:0000313|Proteomes:UP000193467}; RG DOE Joint Genome Institute; RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A., RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B., RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D., RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W., RA Visel A., Grigoriev I.V.; RT "Pervasive Adenine N6-methylation of Active Genes in Fungi."; RL Submitted (JUL-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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. 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:ORY85339.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MCGR01000016; ORY85339.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1Y2FN34; -. DR STRING; 106004.A0A1Y2FN34; -. DR InParanoid; A0A1Y2FN34; -. DR OrthoDB; 5485745at2759; -. DR Proteomes; UP000193467; 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 FunFam; 3.60.20.10:FF:000005; Proteasome subunit beta type-2; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Hydrolase {ECO:0000313|EMBL:ORY85339.1}; KW Protease {ECO:0000256|ARBA:ARBA00022698}; KW Proteasome {ECO:0000256|ARBA:ARBA00022942}; KW Reference proteome {ECO:0000313|Proteomes:UP000193467}; KW Threonine protease {ECO:0000256|ARBA:ARBA00022698}. FT DOMAIN 224..258 FT /note="Proteasome beta subunit C-terminal" FT /evidence="ECO:0000259|Pfam:PF12465" FT ACT_SITE 33 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1" SQ SEQUENCE 281 AA; 29658 MW; 024FE25EFBAD3B24 CRC64; MSSQTGFDFS NNLRNNTLGK RNLALPKATS TGTTIVGCLF DGGIVIGADT RATEGPIVAD KNCEKIHYIS ESIRCAGAGT AADTEFTTAL ISSNIALHAL STGRKPMVVT AMTMLKQMLF QHQGQIGAAL VLGGIDASGP HLYTIAPHGS TDKLPYVTMG SGSLAAMAVF ESSWTPKMSR QAAIDIVCEA IEAGIWNDLG SGSNVDVCVI EPEGTEMLRN YRTPNEKVKK EKSYKWRRGV TAWTKEEVKH FVVASEETVV AGGKVSGPEG TGAGAAMEVD A //