ID   PRS6B_ENCCU             Reviewed;         387 AA.
AC   Q8SQI9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=26S proteasome regulatory subunit 6B homolog;
GN   OrderedLocusNames=ECU08_1970;
GN   and
GN   OrderedLocusNames=ECU10_0130;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which
CC       degrades poly-ubiquitinated proteins in the cytoplasm and in the
CC       nucleus. It is essential for the regulated turnover of proteins and for
CC       the removal of misfolded proteins. The proteasome is a multicatalytic
CC       proteinase complex that 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 (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:0000250}. Nucleus {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; AL590448; CAD26499.1; -; Genomic_DNA.
DR   EMBL; AL590449; CAD25732.1; -; Genomic_DNA.
DR   RefSeq; NP_586128.1; NM_001041961.1.
DR   RefSeq; NP_597323.1; NM_001041932.1.
DR   AlphaFoldDB; Q8SQI9; -.
DR   SMR; Q8SQI9; -.
DR   STRING; 284813.Q8SQI9; -.
DR   PRIDE; Q8SQI9; -.
DR   GeneID; 859745; -.
DR   GeneID; 859774; -.
DR   KEGG; ecu:ECU08_1970; -.
DR   KEGG; ecu:ECU10_0130; -.
DR   VEuPathDB; MicrosporidiaDB:ECU08_1970; -.
DR   VEuPathDB; MicrosporidiaDB:ECU10_0130; -.
DR   HOGENOM; CLU_000688_2_0_1; -.
DR   InParanoid; Q8SQI9; -.
DR   OMA; AYAAQVK; -.
DR   OrthoDB; 571919at2759; -.
DR   Proteomes; UP000000819; Chromosome VIII.
DR   Proteomes; UP000000819; Chromosome X.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0036402; F:proteasome-activating activity; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR005937; 26S_Psome_P45-like.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR   InterPro; IPR035256; PSMC4.
DR   PANTHER; PTHR23073:SF120; PTHR23073:SF120; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome;
KW   Reference proteome.
FT   CHAIN           1..387
FT                   /note="26S proteasome regulatory subunit 6B homolog"
FT                   /id="PRO_0000084695"
FT   BINDING         175..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   387 AA;  43334 MW;  15704091F611D372 CRC64;
     MSARLKGGLF VRYKQMERKL RLLEIREGYV RKEIETLKRE ERHSREELDR VKSVPLIMGQ
     FLEPIDSSTA IVGSTAGSNF VVRILSTVDR ELLKPNTTVA LHRHSSAIVG VLPPEVDSTI
     PVMGESEKPS VTYGDVGGLD VQKQEIKETV ELPLLQSDLY RQIGIDPPQG VLLYGPPGTG
     KTMLVKAVAN HTKATFIRVN GSEFVQKYLG EGPRMVRDVF RLAREKAPSI VFIDEVDSIA
     TKRFDASTSA DREVQRVLIE LLNQMDGFDP AANVKVIMAT NRADTIDPAL LRPGRLDRKI
     EFPLPDRRQK RLVFNAITSK MSLNDSVDIE SLVCRPEKIS CADINSICQE AGMLAVRASR
     YMVTQRDFEE AYSKVVERSG TQPAFYN