ID   A0A1Y2FN34_9BASI        Unreviewed;       281 AA.
AC   A0A1Y2FN34;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   07-OCT-2020, entry version 7.
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   -!- 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}.
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DR   EMBL; MCGR01000016; ORY85339.1; -; Genomic_DNA.
DR   OrthoDB; 977476at2759; -.
DR   Proteomes; UP000193467; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 cellular protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000243; Pept_T1A_subB.
DR   InterPro; IPR035216; Proteasome_beta7.
DR   InterPro; IPR024689; Proteasome_bsu_C.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF44; PTHR11599:SF44; 1.
DR   Pfam; PF12465; Pr_beta_C; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ORY85339.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193467}.
FT   DOMAIN          224..257
FT                   /note="Pr_beta_C"
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
//