ID   PB6LB_SALSA             Reviewed;         217 AA.
AC   A7KII6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Proteasome subunit beta type-6-B like protein;
DE            EC=3.4.25.1;
DE   AltName: Full=Low molecular mass protein 2-delta-B;
DE   Flags: Precursor;
GN   Name=psmb6l-b; Synonyms=lmp2-delta-b;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17651474; DOI=10.1186/1471-2164-8-251;
RA   Lukacs M.F., Harstad H., Grimholt U., Beetz-Sargent M., Cooper G.A.,
RA   Reid L., Bakke H.G., Phillips R.B., Miller K.M., Davidson W.S., Koop B.F.;
RT   "Genomic organization of duplicated major histocompatibility complex class
RT   I regions in Atlantic salmon (Salmo salar).";
RL   BMC Genomics 8:251-251(2007).
CC   -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC       is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC       Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC       pH. The proteasome has an ATP-dependent proteolytic activity. This
CC       subunit is involved in antigen processing to generate class I binding
CC       peptides (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1;
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.
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; EF427379; ABQ59652.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7KII6; -.
DR   SMR; A7KII6; -.
DR   STRING; 8030.ENSSSAP00000035269; -.
DR   MEROPS; T01.013; -.
DR   Proteomes; UP000087266; Genome assembly.
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:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000243; Pept_T1A_subB.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
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; Hydrolase; Immunity; Nucleus; Protease; Proteasome;
KW   Reference proteome; Threonine protease; Zymogen.
FT   PROPEP          1..16
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000341326"
FT   CHAIN           17..217
FT                   /note="Proteasome subunit beta type-6-B like protein"
FT                   /id="PRO_0000341327"
FT   ACT_SITE        17
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  23208 MW;  FA17D10CB66EBCE2 CRC64;
     MERHFMDSQI KGVSTGTTIL AVTFNGGVII GSDSRASIGG SYVSSKTINK LIQVHDRIFC
     CIAGSLADAQ AVTKAAKFQI SFHSIQMESP PLVKAAASVL KELCYNNKEE LQAGFITAGW
     DRKKGPQVYT VALGGMLLSQ PFTIGGSGST YIYGYADAKY KPDMSKEECL QFATNALALA
     MGRDNVSGGV AHLVVITEEG VEHVVIPGDK LPKFHDE