ID A0A384BG11_BALAS Unreviewed; 273 AA.
AC A0A384BG11;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN Name=PSMB10 {ECO:0000313|RefSeq:XP_007198214.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007198214.1};
RN [1] {ECO:0000313|RefSeq:XP_007198214.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007198214.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198};
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}.
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DR RefSeq; XP_007198214.1; XM_007198152.1.
DR AlphaFoldDB; A0A384BG11; -.
DR STRING; 310752.A0A384BG11; -.
DR KEGG; bacu:103016980; -.
DR CTD; 5699; -.
DR InParanoid; A0A384BG11; -.
DR OrthoDB; 5485745at2759; -.
DR Proteomes; UP000261681; Unplaced.
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:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR CDD; cd03763; proteasome_beta_type_7; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR024689; Proteasome_bsu_C.
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:SF4; PROTEASOME SUBUNIT BETA TYPE-7; 1.
DR Pfam; PF12465; Pr_beta_C; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
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|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004203};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681}.
FT DOMAIN 231..267
FT /note="Proteasome beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12465"
FT ACT_SITE 40
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 273 AA; 29216 MW; 6201F217D3230EF2 CRC64;
MQKTALEPQK GFSFENCERN AALERSLPGL RVPHARKTGT TIAGLVFRDG VILGADTRAT
NDSIVAYQSC EKIHFIAPKI YCCGAGVAAD AEMTTRMAAS NMELHALSTG REPRVATVTR
ALRQTLLRYR GFVAASLIVG GVDFTGPQLY SVHPHGSYSR LPFTALGSGQ DAALAVLEDR
FQPNMTLEAA QELLVEAITA GILGDLGSGG SVDACVITGT SAKLLRTLSS PTEPIERSRQ
YRFAPGTTAV LSETVMPLTL ELLEETVQDM DVE
//