ID   PSB6_SCHPO              Reviewed;         225 AA.
AC   Q9UQY2;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=Probable proteasome subunit beta type-6;
GN   Name=pam1; ORFNames=SPAC22F8.06;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 38364 / 968;
RA   Kitamura K., Tsujimoto K., Yamashita I., Shimoda C.;
RT   "Switch from mitotic to meiotic cell cycle is disturbed by strong
RT   activation of Ras-MAP kinase cascade in the fission yeast 26S proteasome-
RT   related mutants.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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       ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; AB012135; BAA88692.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB52716.1; -; Genomic_DNA.
DR   PIR; T38196; T38196.
DR   RefSeq; NP_594729.1; NM_001020157.2.
DR   AlphaFoldDB; Q9UQY2; -.
DR   SMR; Q9UQY2; -.
DR   BioGRID; 278540; 9.
DR   STRING; 284812.Q9UQY2; -.
DR   MEROPS; T01.A12; -.
DR   iPTMnet; Q9UQY2; -.
DR   MaxQB; Q9UQY2; -.
DR   PaxDb; 4896-SPAC22F8-06-1; -.
DR   EnsemblFungi; SPAC22F8.06.1; SPAC22F8.06.1:pep; SPAC22F8.06.
DR   GeneID; 2542062; -.
DR   KEGG; spo:SPAC22F8.06; -.
DR   PomBase; SPAC22F8.06; pam1.
DR   VEuPathDB; FungiDB:SPAC22F8.06; -.
DR   eggNOG; KOG0179; Eukaryota.
DR   HOGENOM; CLU_035750_1_0_1; -.
DR   InParanoid; Q9UQY2; -.
DR   OMA; MLYYKRF; -.
DR   PhylomeDB; Q9UQY2; -.
DR   Reactome; R-SPO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-SPO-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-SPO-5689603; UCH proteinases.
DR   Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q9UQY2; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:PomBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:PomBase.
DR   CDD; cd03757; proteasome_beta_type_1; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
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:SF2; PROTEASOME SUBUNIT BETA TYPE-1; 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; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..225
FT                   /note="Probable proteasome subunit beta type-6"
FT                   /id="PRO_0000148041"
SQ   SEQUENCE   225 AA;  25082 MW;  BE62FA28F9D7D661 CRC64;
     MSQSQFDPYV QNGGTTVAIA GDGFAILAGD TRSVNGYNIN TRFQPRVHEV GDDLVIGASG
     FEADALALVK RIQQRIDLYH DNHERKMSAQ SCACMVRTLL YGKRFFPYYV YTTVAGIDKE
     GKGEIYSFDP VGSYEREWCR AGGSAANFIT PFLDNQVNLH NQYVPGSHGK ERKPRRLLKL
     EEAMKITTDA FTSAGERHIE VGDSVLVKII TKEGVETRII PLKKD
//