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Database: UniProt
Entry: A0A365MLB8_GIBIN
LinkDB: A0A365MLB8_GIBIN
Original site: A0A365MLB8_GIBIN 
ID   A0A365MLB8_GIBIN        Unreviewed;       259 AA.
AC   A0A365MLB8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN   ORFNames=BFJ72_g8012 {ECO:0000313|EMBL:RKL36811.1}, FPRO05_06488
GN   {ECO:0000313|EMBL:RBA09351.1};
OS   Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=948311 {ECO:0000313|EMBL:RBA09351.1, ECO:0000313|Proteomes:UP000251714};
RN   [1] {ECO:0000313|EMBL:RBA09351.1, ECO:0000313|Proteomes:UP000251714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITEM 2341 {ECO:0000313|EMBL:RBA09351.1,
RC   ECO:0000313|Proteomes:UP000251714};
RA   Almiman B.F., Shittu T.A., Muthumeenakshi S., Baroncelli R.,
RA   Sreenivasaprasada S.;
RT   "Genome sequence of the mycotoxigenic crop pathogen Fusarium proliferatum,
RT   strain ITEM 2341 from Date Palm.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RKL36811.1, ECO:0000313|Proteomes:UP000283569}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fp_A8 {ECO:0000313|EMBL:RKL36811.1,
RC   ECO:0000313|Proteomes:UP000283569};
RX   PubMed=30202022; DOI=10.1038/s41598-018-30335-7;
RA   Armitage A.D., Taylor A., Sobczyk M.K., Baxter L., Greenfield B.P.,
RA   Bates H.J., Wilson F., Jackson A.C., Ott S., Harrison R.J., Clarkson J.P.;
RT   "Characterisation of pathogen-specific regions and novel effector
RT   candidates in Fusarium oxysporum f. sp. cepae.";
RL   Sci. Rep. 8:13530-13530(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   -!- 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:RBA09351.1}.
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DR   EMBL; PKMI01000083; RBA09351.1; -; Genomic_DNA.
DR   EMBL; MRDB01000027; RKL36811.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365MLB8; -.
DR   Proteomes; UP000251714; Unassembled WGS sequence.
DR   Proteomes; UP000283569; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProt.
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}.
SQ   SEQUENCE   259 AA;  28679 MW;  464F321256E64E2A CRC64;
     MGSFPASVDA QRYSLRRACL LGCYCWTLKE AEQLLGTTPP QQHINFSSTT FQIIVNMEVL
     LGITGKDFTI IAASKAAMRG ATILKASDDK TRALNKHTLL AFSGEAGDTV QFAEYIQRNA
     QLYSMRNESD LSPSGLAHFV RGELATSLRS RKPYNVNLLM GGVDPITGKP SLYWLDYLAS
     LADVPYAAHG YAQYYCLSIL DKHHHPDITL HQGIKILTMC TDELKRRLPI DFKGMVVKAV
     KADGIVDIEF DDDKVVKCA
//
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