ID   PSB3_GIAIN              Reviewed;         207 AA.
AC   Q9N9W8;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Proteasome subunit beta type-3;
GN   Name=PRSBETA3;
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Portland-1;
RA   Emmerlich V., Riekenberg S., Bakker-Grunwald T., Scholze H.;
RT   "Evidence for the existence of a 26S proteasome in Giardia lamblia.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
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; AJ297366; CAB97490.1; -; mRNA.
DR   VEuPathDB; GiardiaDB:DHA2_13756; -.
DR   VEuPathDB; GiardiaDB:GL50581_1828; -.
DR   VEuPathDB; GiardiaDB:GL50803_0013756; -.
DR   VEuPathDB; GiardiaDB:QR46_2707; -.
DR   eggNOG; KOG0180; Eukaryota.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03759; proteasome_beta_type_3; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR033811; Proteasome_beta_3.
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:SF11; PROTEASOME CORE PARTICLE SUBUNIT BETA 3; 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.
FT   CHAIN           1..207
FT                   /note="Proteasome subunit beta type-3"
FT                   /id="PRO_0000148063"
SQ   SEQUENCE   207 AA;  23022 MW;  F9D8025ADD5E5647 CRC64;
     MGNIWEYNGS ALIGIKGXDC VALAADKRLG CSYQTLTIGN EERIFRLSQS CLLGLAGLQT
     DVLTTYRQIR MKSNLYHLQE DREIRPRATA KMISSFLYKH RFGPYFISPI IAGFEADGKP
     YLGAMDTIGC LDDCTNFQIA GTASDFLLGL CETHVKPDMS EDEILPLMEQ IIRSATNRDA
     YSGWGAHVVV LRRDGTTSDI PISTRMD
//