ID   PSB1B_CARAU             Reviewed;         237 AA.
AC   Q9IB83;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Proteasome subunit beta type-1-B;
DE   AltName: Full=20S proteasome beta-6 subunit B;
DE            Short=B6-B;
GN   Name=psmb1-B;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=10781806; DOI=10.1016/s0014-5793(00)01441-1;
RA   Tokumoto M., Yamaguchi A., Nagahama Y., Tokumoto T.;
RT   "Identification of the goldfish 20S proteasome beta6 subunit bound to
RT   nuclear matrix.";
RL   FEBS Lett. 472:62-66(2000).
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   ---------------------------------------------------------------------------
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; AB035497; BAA95592.1; -; mRNA.
DR   AlphaFoldDB; Q9IB83; -.
DR   SMR; Q9IB83; -.
DR   Proteomes; UP000515129; Genome assembly.
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; ISS:UniProtKB.
DR   GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR035202; Proteasome_beta1.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF59; PTHR11599:SF59; 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   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..237
FT                   /note="Proteasome subunit beta type-1-B"
FT                   /id="PRO_0000148034"
SQ   SEQUENCE   237 AA;  26002 MW;  1E7C5B8A62789CC6 CRC64;
     MISAQACGAN GKMKDYHYSG PVEHKFSPYA FNGGTVLAVA GEDFALVASD TRLSEGYSIH
     SRDSPKCYKL TDTTVIGCSG FHGDCLTLTK IIEARLKMYK HSNNKSMTSG AIAAMLSTIL
     YGRRFFPYYV YNIIGGLDEE GRGAVYSFDP VGSYQRDTYK AGGSASAMLQ PLLDNQIGFK
     NMENVEQVPL SQEKAVQLVK DVFISAAERD VYTGDALKIC IITKEGIREE IVPLRKD