ID   PSB1A_CARAU             Reviewed;         238 AA.
AC   Q9IB84;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   22-FEB-2023, entry version 86.
DE   RecName: Full=Proteasome subunit beta type-1-A;
DE   AltName: Full=20S proteasome beta-6 subunit A;
DE            Short=B6-A;
GN   Name=psmb1-A;
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}.
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DR   EMBL; AB035496; BAA95591.1; -; mRNA.
DR   AlphaFoldDB; Q9IB84; -.
DR   SMR; Q9IB84; -.
DR   Ensembl; ENSCART00000099382; ENSCARP00000090380; ENSCARG00000044527.
DR   OrthoDB; 158278at2759; -.
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:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..238
FT                   /note="Proteasome subunit beta type-1-A"
FT                   /id="PRO_0000148033"
SQ   SEQUENCE   238 AA;  26175 MW;  048C08CD7434C886 CRC64;
     MMISAQACGA NGRMKDYHYT GPVEHKFSPY AFNGGTVLAV AGEDFALVAS DTRLSEGYSI
     HSRDSPKCYK LTDTTVIGCS GFHGDCLTLT KIIEARLKMY KHSNNKSMTS GAIAAMLSTI
     LYGRRFFPYY VYNIIGGLDE EGRGAVYSFD PVGSYQRDTY KAGGSASAML QPLLDNQIGF
     KNMENVEQVP LSQEKAVQLV KDVFISAAER DVYTGDALKI CIITKEGIRE EIVPLRKD
//