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Database: UniProt
Entry: J9VN10_CRYNH
LinkDB: J9VN10_CRYNH
Original site: J9VN10_CRYNH 
ID   J9VN10_CRYNH            Unreviewed;       303 AA.
AC   J9VN10;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 2.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=proteasome endopeptidase complex {ECO:0000256|ARBA:ARBA00012039};
DE            EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039};
GN   ORFNames=CNAG_02725 {ECO:0000313|EMBL:AFR93964.2};
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR93964.2, ECO:0000313|Proteomes:UP000010091};
RN   [1] {ECO:0000313|EMBL:AFR93964.2, ECO:0000313|Proteomes:UP000010091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC   {ECO:0000313|Proteomes:UP000010091};
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA   Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA   Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA   Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA   Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA   Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA   Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198};
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DR   EMBL; CP003822; AFR93964.2; -; Genomic_DNA.
DR   RefSeq; XP_012047922.1; XM_012192532.1.
DR   AlphaFoldDB; J9VN10; -.
DR   GeneID; 23886288; -.
DR   KEGG; cng:CNAG_02725; -.
DR   VEuPathDB; FungiDB:CNAG_02725; -.
DR   HOGENOM; CLU_035750_3_0_1; -.
DR   OrthoDB; 5485745at2759; -.
DR   Proteomes; UP000010091; Chromosome 3.
DR   GO; GO:0005839; C:proteasome core complex; 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; 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   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   4: Predicted;
KW   Proteasome {ECO:0000313|EMBL:AFR93964.2}.
FT   DOMAIN          236..269
FT                   /note="Proteasome beta subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12465"
SQ   SEQUENCE   303 AA;  31868 MW;  225C2EF04206D7F9 CRC64;
     MTKLAETPSV GFDFSNFARN QFLGQRLQGI PKATSTGTTI VGVIYGGGSS GEEPGVCLGA
     DTRATGGPIV ADKNCEKIHY LAPHIRCCGA GTAADTEFVT NLISSNLELH ALSQGRQARI
     VTAMTMLKQY LFRYQGHVGA HLVLGGVDAT GPQLFTVHAH GSTDKLPYVT MGSGSLAAMA
     VFESSFKEHM TRQEAIDLVA RAIRSGVFND LGSGSNVDVA VITKNGTEML RNYQTPNERG
     LKSRNYKFRR GTTAWTKESV RSLIVKEEVK STTGAGKAQG AAEAIPVAAG AGPGGAEGMD
     IDG
//
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