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Database: UniProt
Entry: A0A1Y1V3H7_9FUNG
LinkDB: A0A1Y1V3H7_9FUNG
Original site: A0A1Y1V3H7_9FUNG 
ID   A0A1Y1V3H7_9FUNG        Unreviewed;       195 AA.
AC   A0A1Y1V3H7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN   ORFNames=BCR36DRAFT_331713 {ECO:0000313|EMBL:ORX46375.1};
OS   Piromyces finnis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces.
OX   NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX46375.1, ECO:0000313|Proteomes:UP000193719};
RN   [1] {ECO:0000313|EMBL:ORX46375.1, ECO:0000313|Proteomes:UP000193719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT   biomass hydrolysis.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORX46375.1, ECO:0000313|Proteomes:UP000193719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
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 (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- FUNCTION: Non-catalytic component of the proteasome, a multicatalytic
CC       proteinase complex which is characterized by its ability to cleave
CC       peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group
CC       at neutral or slightly basic pH. The proteasome has an ATP-dependent
CC       proteolytic activity. {ECO:0000256|ARBA:ARBA00024953}.
CC   -!- SUBUNIT: Component of the proteasome complex.
CC       {ECO:0000256|RuleBase:RU004203}.
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   -!- 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}.
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:ORX46375.1}.
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DR   EMBL; MCFH01000035; ORX46375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1V3H7; -.
DR   STRING; 1754191.A0A1Y1V3H7; -.
DR   EnsemblFungi; ORX46375; ORX46375; BCR36DRAFT_331713.
DR   OrthoDB; 158209at2759; -.
DR   Proteomes; UP000193719; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IEA:EnsemblFungi.
DR   GO; GO:0061133; F:endopeptidase activator activity; IEA:EnsemblFungi.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   CDD; cd03758; proteasome_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; IPR035206; Proteasome_beta2.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR   PANTHER; PTHR11599:SF6; PROTEASOME SUBUNIT BETA TYPE-2; 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:UP000193719}.
SQ   SEQUENCE   195 AA;  22219 MW;  2286FC775003D2DE CRC64;
     MEVLLGIQGK DFVLVASDAL AITSIVAMKR NHNKTRKLND NVLLMFSGEG GDSVQFCEFI
     QRNVQLNGIR RGYPLSTKAA ANFTRVELAE SLRSRHPYQV NLLIAGCDPD TGVPELYWMD
     YLASLKKLPF AVQGYGQYFC NSTMDRYYRP DMNLEEAKAL MKKCINELKV RFIINFSDFV
     FQVVDKDGIK EIKLE
//
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