ID   PSB4_PICGU              Reviewed;         194 AA.
AC   A5DB52; Q6YJJ9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Probable proteasome subunit beta type-4;
GN   Name=PRO2; ORFNames=PGUG_00507;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
RX   PubMed=15925311; DOI=10.1016/j.femsyr.2005.03.007;
RA   Boretsky Y.R., Kapustyak K.Y., Fayura L.R., Stasyk O.V., Stenchuk M.M.,
RA   Bobak Y.P., Drobot L.B., Sibirny A.A.;
RT   "Positive selection of mutants defective in transcriptional repression of
RT   riboflavin synthesis by iron in the flavinogenic yeast Pichia
RT   guilliermondii.";
RL   FEMS Yeast Res. 5:829-837(2005).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC       Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN08876.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CH408155; EDK36409.1; -; Genomic_DNA.
DR   EMBL; AY138984; AAN08876.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; XP_001487130.1; XM_001487080.1.
DR   AlphaFoldDB; A5DB52; -.
DR   SMR; A5DB52; -.
DR   STRING; 4929.XP_001487130.1; -.
DR   MEROPS; T01.984; -.
DR   EnsemblFungi; EDK36409; EDK36409; PGUG_00507.
DR   GeneID; 5129627; -.
DR   KEGG; pgu:PGUG_00507; -.
DR   VEuPathDB; FungiDB:PGUG_00507; -.
DR   eggNOG; KOG0177; Eukaryota.
DR   HOGENOM; CLU_035750_12_0_1; -.
DR   InParanoid; A5DB52; -.
DR   OMA; RMCTDEL; -.
DR   OrthoDB; 1392180at2759; -.
DR   Proteomes; UP000001997; 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; ISS:UniProtKB.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IEA:UniProt.
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; -; 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:SF6; PTHR11599:SF6; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR   PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..194
FT                   /note="Probable proteasome subunit beta type-4"
FT                   /id="PRO_0000295032"
SQ   SEQUENCE   194 AA;  21766 MW;  4D7964E1660B0634 CRC64;
     MDIVLGIRVE DCTLVATSKA ATRGISVLKD TDDKTRQLNS HNLMAYSGEA GDTVQFAEYI
     QANTQLYTMR ENDTELSPKA TASFVRNQLA TSIRSRKPYQ VNVLLAGYDT NTGKPSLNWI
     DYLGTQVELP YAAHGYAGFY CTSLLDKHYK KGMNFEDGLD LLKKCIKELE TRMPIDFKGC
     YIKVVDKEGI KLVE