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Database: UniProt
Entry: A0A316YLR4_9BASI
LinkDB: A0A316YLR4_9BASI
Original site: A0A316YLR4_9BASI 
ID   A0A316YLR4_9BASI        Unreviewed;       209 AA.
AC   A0A316YLR4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN   ORFNames=FA10DRAFT_268124 {ECO:0000313|EMBL:PWN89598.1};
OS   Acaromyces ingoldii.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX   NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN89598.1, ECO:0000313|Proteomes:UP000245768};
RN   [1] {ECO:0000313|EMBL:PWN89598.1, ECO:0000313|Proteomes:UP000245768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN89598.1,
RC   ECO:0000313|Proteomes:UP000245768};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- FUNCTION: Component of the proteasome, a multicatalytic proteinase
CC       complex which is characterized by its ability to cleave peptides with
CC       Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC       slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC       activity. {ECO:0000256|RuleBase:RU004203}.
CC   -!- SUBUNIT: Component of the proteasome complex.
CC       {ECO:0000256|RuleBase:RU004203}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}.
CC       Nucleus {ECO:0000256|RuleBase:RU004203}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family.
CC       {ECO:0000256|RuleBase:RU004203}.
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DR   EMBL; KZ819637; PWN89598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316YLR4; -.
DR   STRING; 215250.A0A316YLR4; -.
DR   InParanoid; A0A316YLR4; -.
DR   OrthoDB; 1104143at2759; -.
DR   Proteomes; UP000245768; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03759; proteasome_beta_type_3; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR033811; Proteasome_beta_3.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR   PANTHER; PTHR32194:SF5; PROTEASOME SUBUNIT BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU004203};
KW   Nucleus {ECO:0000256|RuleBase:RU004203};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245768}.
SQ   SEQUENCE   209 AA;  23121 MW;  885067B143A07663 CRC64;
     MSIMEYNGGS VVAMKGKNCV AIASDLRLGQ QAMTVACNFD KVFAVTERTY LGLPGLASDV
     ATLKETFRYR VNMYKMKEER EIQPETFAHL VSSTLYEKRF GPYFIEPVIC GLSSPDAPVP
     NEPFIAASDL IGCLNFAKDF VVSGTASDKL FGMAEGLWEE DLGPEELFET ISQTLLGALE
     RDALSGWGAI VRVITPEKVT ERWLKSRQD
//
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