ID R7SC42_TREMS Unreviewed; 270 AA.
AC R7SC42;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN ORFNames=TREMEDRAFT_46043 {ECO:0000313|EMBL:EIW65807.1};
OS Tremella mesenterica (strain ATCC 24925 / CBS 8224 / DSM 1558 / NBRC 9311 /
OS NRRL Y-6157 / RJB 2259-6 / UBC 559-6) (Jelly fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Tremellaceae; Tremella.
OX NCBI_TaxID=578456 {ECO:0000313|EMBL:EIW65807.1, ECO:0000313|Proteomes:UP000054539};
RN [1] {ECO:0000313|Proteomes:UP000054539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fries {ECO:0000313|Proteomes:UP000054539};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH711546; EIW65807.1; -; Genomic_DNA.
DR RefSeq; XP_007008275.1; XM_007008213.1.
DR AlphaFoldDB; R7SC42; -.
DR GeneID; 18493833; -.
DR KEGG; tms:TREMEDRAFT_46043; -.
DR VEuPathDB; FungiDB:TREMEDRAFT_46043; -.
DR eggNOG; KOG0179; Eukaryota.
DR OrthoDB; 158278at2759; -.
DR Proteomes; UP000054539; 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 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 {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:UP000054539}.
FT REGION 247..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 270 AA; 29770 MW; CAEB51928469A10A CRC64;
MTLLAQSPMS LHDTYAAPVE HRFNPYSENG GTILAIAGAD FSVIAGDTRQ SEGYSIQTRY
ARKVFQLTDN AVLATNGFAA DGKNFVRRLK QSLEWYQHNH HKQMGLKAIA RLIQTMLYGR
RFFPYYVYNI LGGIEEDGSG AVYSFDPVGS YEREACRAAG AAQALVQPFL DNQIYFKNQQ
PEPGAEPFVP GRLPLSTVLG LVVDSFTSAT ERHIEVGDGI EIFIVMAKGR SPESLLDEKL
GEGMTIEEVP PVGEGGEERT FLLSGPLKRD
//
